studium 0.18.7

data/lib/studium/exam_topics/strukturbiologie

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+# =========================================================================== #
+# === Strukturbiologie
+#
+# Struktur und Funktion der Proteine. (folding tag)
+#
+# Struktur tag. Structure tag. Strukturbio tag. Protein Tag.
+# Struk tag. Röntgen tag, X-ray tag. Strukt tag.
+# Strukturbiologie tag.
+# =========================================================================== #
+
+- <one>Wavelength</one> <two>of X-rays</two>, <three>in nm</three>? <one>0.1 nm</one> - thus <two>very, very low</two>. []
+- Ist die <one>Metallbindung</one> ein <two>strukturstabilisierender Faktor</two>? <one>Ja</one> - zum Beispiel <two>Zink</two> bei den <three>Zinkfingerproteinen</three>. []
+- Ordne die 20 Aminosäuren nach ihrer <one>Hydrophobizität</one>, <two>beginnend mit der hydrophobsten Aminosäure</two>. A: <one>IVL-FCM-AGT-SWY-PHE-QDN-KR</one>.
+- In <one>structural biology</one>: what is meant with the term <two>docking</two>? The term docking refers to <one>the interaction between proteins</one>.
+- Welche <one>Ladung</one> tragen <two>die beiden Termini eines Proteins</two> <three>bei neutralem pH</three>? Beide sind geladen, als <one>NH₃⁺</one> und <one>COO⁻</one>.
+- Die <one>Bindungsstärke zwischen Protein und Ligand</one> wird ... genannt. A: <one>Affinität</one>.
+- In der Biochemie: was benötigen <one>parallele Beta-Stränge</one>? Eine <one>Überkreuzverbindung</one>. []
+- The <one>average weight of an aminoacid</one> <two>bound in a protein</two> <three>is ... </three>? <one>110 Dalton</one>. []
+- Benenne <one>eine Substanz</one> die zur Ausfällung und Kristallisierung von einem Protein, im Labor, genutzt wird. A: <one>Ammoniumsulfat</one>.
+- The <one>zona pellucida domain</one> consists of approximately n amino acids? About 260 amin acids.
+- Is the <one>hydrophobic effect</one> temperature-dependent? Yes - it is <one>strongly temperature-dependent</two>.
+- In a <one>mutagenesis experiment</one> in structural biology, a hydrogen-bonded side chain can be replaced by a side chain which cannot form hydrogen bonds. Give a specific example on the level of aminoacids here. A: Replacing <one>tyrosine</one> (Y) with <two>phenylalanine</two> (F).
+- <one>Protein stability</one> is affected through environmental factors. Name three such factors. A: (1) <one>temperature</one> (2) <one>pH</one> (3) <one>salt concentration</one>
+- Do <one>hydrogen bonds</one> help <two>stabilize protein structure</two>? <one>Yes</one>.
+- Die Röntgenstrukturanalyse hilft immens bei der Erstellung von dreidimensionalen Elektronendichtekarten. Dabei wird eine Auflösung von n nm erreicht? Von 0.5 nm.
+- <one>Welche Substanz</one> wird häufig verwendet um ein bestimmtes Protein auszufällen und zu kristallisieren? <one>Ammoniumsulfat</one>.
+- Is the <one>protein interior</one> <two>liquid-like</two>? <one>No</one>.
+- Schafft die <one>Röntgenstrukturanalyse</one> eine Auflösung von <two>0.1nm</two>? <one>Ja</one>.
+- Compare small and large proteins in regards to their ability to renature, after denaturation. A: Small proteins are often able to renature under certain conditions. For larger proteins this is rarely the case.
+- <one>The sidechains of two aminoacids</one> <two>with positive and negative charge</two> can approach one another in space, to form ... ? <one>A salt bridge</one>. URL: https://en.wikipedia.org/wiki/Salt_bridge_(protein_and_supramolecular)
+- Proteine können auf <two>Ligandenbindung</two> mit einer <one>Konformationsänderung</one> reagieren. <three>Nenne hierzu ein Protein-Beispiel</three>. A: <one>Calmodulin</one>.
+- Spielen <one>Peptidylprolyl-cis</one>/<one>trans-Isomerasen</one> eine Rolle bei der Proteinfaltung? <one>Ja</one>, sogar <two>eine bedeutende Rolle</two>.
+- <one>Wie</one> bestimmt man den <two>isoelektrischen Punkt</two> <three>von Proteinen</three> experimentell? Mit Hilfe einer <one>Titrationskurve</one>. URL: https://de.wikipedia.org/wiki/S%C3%A4ure-Base-Titration#Verlauf_von_Titrationskurven
+- Name <one>the three most common obstacles to correct folding</one>. A: (1) aggregation of the intermediate through exposed hydrophobic groups (2) <one>formation of incorrect disulfide bonds</one> (3) <one>isomerization of proline residues</one>
+- <one>Durchmesser</one> der <two>Alpha-Helix</two>, <three>in Angstrom</three>? <one>14 Angstrom</one>.
+- How is the <one>winged HTH domain</one> different from the (regular) <two>HTH domain</two>? The <one>winged HTH domain</one> has a longer turn, e. g. the <two>winged turn</two>, <three>which is 10 aminoacids in length</three>.
+- One of <one>the most fundamental question</one> <two>about a protein is ... </two>? Its (natural) <one>function in a cell</one>.
+- Angenommen ein Protein besitzt eine <one>aminoterminale Signalsequenz</one> - <two>was können wir draus schließen</two>? Das dieses Protein zur <one>Sekretion</one> bestimmt sein mag.
+- Give an archetypical example for a <one>globular protein</one> (in a solution) and a <two>membrane protein</two> (in a membrane). A: (1) globular protein: <two>myoglobin</two> (2) membrane protein: <two>aquaporin</two>
+- The <one>Ramachandran Plot</one> shows the ... angles in proteins. A: The <one>allowed backbone torsion angles</one> <two>in proteins</two>.
+- Give an example for <one>protective proteins</one>. A: The <one>antibodies</one>.
+- A <one>protein</one> that may recognize external and internal chemical signals, could be called ... ? a <one>receptor</one>.
+- Die Funktion eines Proteins wird generell durch ... bestätigt. A: Durch <one>Experimente</one>.
+- Viele eukaryote Proteine besitzen eine WD40-Domäne. Diese Proteine sind häufig bei welchem zellulären Vorgang beteiligt? Diese Proteine sind häufig an Signalketten beteiligt.
+- Die wohl wichtigsten <one>„Abschaltproteine“</one> in einer Zelle sind ... ? die <one>Proteinphosphatasen</one>.
+- The majority of the proteins have a fibrillar or a globular structure? A <one>globular structure</one>.
+- Does <one>myosin</one> belong to the fibrillar proteins? <one>Yes</one>.
+- Fibrillar proteins are ...-like. A: <one>filament-like</one>.
+- In der Strukturbiologie, in der Proteindomäne <one>WD40</one>: wofür steht W und D? Dies sind die Aminosäuren Tryptophan und Asparaginsäure, die am Ende der Domäne vorgefunden werden können.
+- Länge in der <one>Alpha-Helix</one> pro Aminosäure, <two>in nm</two>? <one>0.16 nm</one>.
+- Ist eine Rotation um eine Peptidbindung möglich? Nein. Eine Rotation um die Peptidbindung ist nicht möglich, da diese partiellen Doppelbindungscharakter (== Doppelbindung) besitzt.
+- <one>Hämoglobin</one> kommt in zwei Konformationen vor T Form und R Form. Welche daovn bindet Sauerstoff sehr gut? Die <one>relaxed Form</one> (R) bindet Sauerstoff gut. 
+- Das Bild das man mit Röntgenstrahlung von einem Proteinkristall gewinnt, wird ... genannt. A: <one>Beugungsbild</one>.
+- Ist <one>Rhodopsin</one> membranassoziiert? Ja, sogar membranintegriert. Es ist ein Lichtrezeptor; somit macht dies Sinn.
+- Ist <one>Kollagen</one> ein Protein? <one>Ja</one> - ein Strukturprotein.
+- Das <one>dominierende Sekundärstrukturelement im Myoglobin</one> ist ... ? die α-Helix.
+- Wenn ein Protein die Lipiddoppelschicht einer Zelle komplett durchspannt, wird es generell ... genannt. A: Dies ist ein <one>integrales Membranprotein</one>.
+- Welches Sequenzmotiv findet sich in allen Mitgliedern der Cytochrom-c-Familie? <one>CXXCH</one>.
+- Sequenzvergleiche von Proteinen spüren ... in verwandten Proteinen auf. A: Schlüsselpositionen.
+- Nenne die zwei wichtigsten Domänen in GADPH. A: (1) NAD+-Bindungsdomäne (2) Substratbindungsdomäne
+- Eine typische Domäne in einem Protein besteht aus (von-bis) Aminosäuren? 100-200 Aminosäuren.
+- Verwende ein anderes Wort für <one>domain shuffling</one>. A: <one>Exon shuffling</one>.
+- Die molekulare Größe von Lysozym beträgt etwa n nm? Etwa 3.3 nm - 4.5 nm.
+- Warum sind <one>Disulfidbrücken</one> sind von großer Bedeutung für die Proteinstruktur? Disulfidbrücken erlauben es Proteinen zusätzliche kovalente Bindungen innerhalb eines Proteins, aber auch zwischen Proteinen, auszubilden.
+- <one>Disordered proteins</one> were shown to be <two>significantly depleted in which amino acid residues in particular</two>? In big <one>aromatic amino acid residues</one> such as <two>Tryptophan</two> (<three>W</three>), <two>Tyrosine</two> (<three>Y</three>) and <two>Phenylalanine</two> (<three>F</three>).
+- The <one>interior of a protein</one> is ...? <one>hydrophobic</one> - proteins thus contain a <two>hydrophobic core</two>.
+- For <one>X-ray</one>, the <two>crystal</two> is mounted between ... ? Between an <one>X-ray source</one> and an <one>X-ray detector</one>.
+- In folding of a protein: what do we mean with a <one>simple two-state equilibrium</one>? This refers to, for example, a simple unfolding when the native protein very quickly unfolds; and refolds also quickly. There is thus <one>no stable intermediate</one>.
+- The <one>ATPase</one> has a <two>F₁F₀ component</two>. <three>What do the lower numbers indicate here</three>? (1) <one>F₁</one> had this name derived from a purification scheme, where this stood for <two>fraction1</two>. (2) <one>F₀</one> got its name from this faction's ability to bind to <two>oligomycin</two>.
+- Does the <one>alpha-helix</one> have a <two>dipole moment</two>? <one>Yes</one> it does.
+- Nenne <one>zwei weitere Struktur-Elemente</one> in der Biochemie außer dem <two>Beta-Faltblatt</two> und der <two>Alpha-Helix</two>. A: (1) <one>omega-loop</one> (2) <one>beta-turn</one>
+- In structural biology: <one>an essential increase in the hydrodynamic volume</one> <two>is associated with ... </two>? With <one>the unfolding of a protein molecule</one>.
+- <one>How</one> are the connections in a protein, created via <two>electrostatic interactions</two>, <three>called ... </three>? A: <one>Salt bridges</one>.
+- The <one>PDB</one> (<two>Protein Data Bank</two>) <three>contained how many proteins</three> in <four>2005</four>? Roughly <one>25.000 proteins</one>, <two>determined primarily by X-ray crystallography</two>.
+- ... stabilisieren die Tertiärstruktur. A: <one>Nichtkovalente Wechselwirkungen</one> <two>stabilisieren die Tertiärstruktur</two>.
+- The <one>secondary structure</one> <two>of a protein</two> depends solely on ...? <one>Hydrogen bonding</one>.
+- <one>Warum</one> sind nicht alle Werte im <two>Ramachandran-Diagramm</two> möglich zwischen phi und psi Bindungswinkeln? Weil es zu <one>Kollisionen zwischen den Atomen</one> kommen kann; dies ist energetisch gesehen ungünstig.
+- <one>Wie</one> werden <two>Sekundärstrukturelemente in Proteinen</two> gebildet? <one>Durch</one> <two>Wechselwirkungen der Peptidbindungen</two>.
+- In der Strukturbiologie: was meinen wir mit einem <one>positiven allosterischen Effekt</one> und mit einem <one>negativen allosterischen Effekt</one>? (1) <one>Positiver allosterischer Effekt</one>: dies ist dann der Fall, wenn die Bindung eines Liganden die Bindung eines <two>anderen</two> <three>Liganden erleichtert</three>. (2) <one>Negativer allosterischer Effekt</one>: dies ist dann der Fall, wenn die Bindung eines Liganden die Bindung eines <two>anderen</two> <three>Liganden erschwert</three>.
+- A <one>fusion tag</one> <two>may act as ... </two>? as <one>a nucleation site for the folding of the target protein</one>.
+- <one>Lipocalins</one> are an <two>eight-stranded barrel</two>. <three>They can bind ... </three>? <one>Retinol</one>. URL: https://en.wikipedia.org/wiki/Lipocalin
+- Was bedeuten <one>weiße Flächen</one> <two>im Ramachandran-Diagramm</two>? Dies sind Bereiche, die infolge starker sterischer Wechselwirkungen <one>unzulässige Torsionswirkel</one> aufweisen.
+- Name <one>the three main methods</one> for <two>structure determination in protein research</two>. A: (1) <one>X-ray crystallography</one> (2) <one>NMR spectroscopy</one> (3) <one>electron microscopy</one>
+- What is the job of the <one>Wiggler</one> <two>in a synchroton</two>? The <one>wiggler</one> <two>increases the intensity of the beam</two>. (Mnemonic: <three>to wiggle the intensity of the beam</three>.)
+- <one>Albumin</one> ist <two>wie groß</two> (<three>von-bis</three>)? <one>65-70 kDa</one>. URL: https://de.wikipedia.org/wiki/Albumine
+- Bei den photometrischen Proteinbestimmungsmethoden wird das Ergebnis mittels einer <one>Kalibrationskurve</one> ermittelt. Diese Kurve wird mit einem reinen Protein erstellt, sehr häufig <two>mit welchem Protein</two>? Mit <one>BSA</one> - <two>bovines Serumalbumin</two> (<three>bovine serum albumin</three>), eben aus dem Rind. URL: https://en.wikipedia.org/wiki/Bovine_serum_albumin
+- Historisch betrachtet: <two>welche Proteine</two> konnten zuerst <one>entdeckt</one> werden? Jene die <one>reichlich</one>, und dadurch <two>einfach zu isolieren</two>, <one>vorhanden waren</one>.
+- <one>G-Proteine</one> werden auch <two>7-Transmembran-Rezeptoren</two> genannt. <three>Warum</three>? Da sie <one>7 Alpha-Helices</one> besitzen.
+- Hat ein Protein einen <one>Schmelzpunkt</one> <two>so deutet dies worauf hin</two>? Das es in einer bestimmten 3D-Struktur vorliegt - also <one>nicht ungefaltet</one> vorliegen kann.
+- <one>Proteins</one> <two>are not static structures</two>. <three>They are best represented by ... </three>? An ensemble of possible conformations.
+- Bei der <one>Bildung einer Peptidbindung zwischen Aminosäuren</one> geht <two>Wasser</two> (<two>H₂0</two>) verloren. <three>Gibt es einen einfachen Weg, wie wir uns merken können, wer diese drei Atome liefert</three>? <one>Ja</one> - und zwar sind die Enden der Aminosäuren innerhalb der Zelle geladen; wir haben also eine <one>-COO (minus)-Gruppe</one> sowie eine <one>-NH3 (⁺)-Gruppe</one>. Daraus folgt das die -COO Gruppe nur ein O liefern kann; und die -NH3 Gruppe nur zwei H-Atome liefern kann.
+- <one>Calmodulin</one> <two>can bind 4x Ca²⁺</two>, which will cause Calmodulin to undergo a conformational change. Which structural motife is responsible for the <two>Ca²⁺-binding</two>, though? A <one>helix-loop-helix</one> (<two>HLH</two>) motife.
+- <one>How simple</one> is it to do unfolding/re-folding reactions, on <two>insulin</two>, in the laboratory? <one>Very difficult</one>; it gives <two>poor yields</two>. Many <three>incorrectly paired disulphide bridges</three> may form.
+- The key of understanding the functional job of proteins lies in ... ? Their <one>shape</one>.
+- Nenne <one>ein konkretes Beispiel</one> für die Tertiärstruktur eines Proteins. A: Eine <one>vollständige Beta-Kette eines Hämoglobins</one>.
+- Are <one>beta-sheets</one> <two>flat</two>? <one>No</one> - most beta-sheets are <two>twisted</two>.
+- Bei dem <one>Einsatz von NMR zwecks Untersuchung der Proteine</one> wird mitunter auch <two>NOE</two> (<three>Nuclear Overhauser Enhancement</three>) verwendet. <four>Dies liefert uns welche Information zusätzlich</four>? <one>NOE</one> liefert uns <two>zusätzliche Rauminformation</two>.
+- <one>Wavelength of X rays</one> <two>in Angstrom</two>, from-to? From about <one>0.5 Angstrom</one> up to <one>1.5 Angstrom</one>. URL: https://en.wikipedia.org/wiki/X-ray
+- Gibt es <one>Proteine</one> <two>ohne 3D-Struktur</two>? <one>Strenggenommen eigentlich nicht</one> - aber allgemein nennen wir eben entfaltete Proteine <two>unfolded</two>.
+- Sind <one>synthetische Polypeptide mit Zufallssequenzen</one> <two>zur Faltung fähig</two>? <one>Nein</one> - <two>sie sind nicht zur Faltung fähig</two>.
+- The <one>upper size limit of NMR</one> applied onto proteins is <two>about n aminoacids</two>? About <one>~350 aminoacids</one> (<two>~40kDa</two>).
+- <one>Warum</one> liefern <two>Röntgenstrahlen</two> die bestmögliche Auflösung? Da <one>die Wellenlänge der Röntgenstrahlen</one> ungefähr der einer <two>kovalenten Bindung</two> entspricht.
+- <one>How</one> does <two>comparative modeling</two> work? <one>Comparative modeling</one> uses an existing 3D structure of a protein to model the geometry of a structurally unknown target with similar amino acid sequence.
+- Does <one>proline</one> <two>contribute to overall folding</two>? <one>Yes</one>, <two>by forming bends</two>.
+- The <one>β-α-β motif</one> <two>is frequently found in ...</two> which proteins? In <one>ion channels</one>.
+- Overall, <one>proteins can be categorized</one> into which two groups based on their overall three-dimensional shape? (1) <one>globular proteins</one> (2) <one>fibrous proteins</one>
+- In <one>structural biology</one>: <two>why</two> was the name TIM chosen for a <three>TIM barrel</three>? <one>TIM</one> stands for <two>triose phosphate isomerase</two>. URL: https://en.wikipedia.org/wiki/TIM_barrel
+- <one>Aequorin</one> <two>can bind which ions</two>? <one>Ca²⁺ ions</one>. It contains three EF hand motifs that can bind calcium.
+- Was heißt es wenn wir sagen das ein Protein <one>atmet</one>? Das <one>ein Protein nicht starr ist</one>, sondern <two>konformationellen Fluktuationen unterliegt</two>.
+- The <one>molten globule</one> should not be viewed as a single structural entity but instead as ...? An <one>ensemble of related structures that are</one> <two>rapidly interconverting</two>.
+- Die <one>CD-Spektroskopie</one> <two>funktioniert bei welcher Aminosäure nicht</two>? <one>Glycin</one>, da diese Aminosäure <two>nicht chiral</two> ist.
+- In general: <one>where</one> <two>in a large protein</two> can we find <three>Alpha-helices</three>? Along the <one>outside surface of a protein</one>.
+- Wie schwer ist ein Protein, das von <one>600 Nukleotiden</one> codiert wird? Dies sind <one>200 Aminosäuren</one>. Das durchschnittliche Gewicht einer Aminosäure in einem Polypeptid ist <two>110 Dalton</two>. Dies bedeutet auch <three>110 Gramm pro Mol</three>. Das mal 200, also 110 x 200 ergibt <four>22.000 Gramm pro Mol</four>.
+- <one>How a protein folds up into its native shape</one> not only dictates how the protein works, but is also important because ... ? Because <one>that protein may interact with other entities</one> (<two>aka other proteins</two>), and thus may have an important biological role in the cellular context.
+- The <one>F1-ATP Synthase component</one> <two>has a diameter of ...</two>? Of <one>9 nm</one>.
+- Why was the name <one>induced fit</one> chosen for the enzyme-substrate interaction? This was chosen because <one>the enzyme is induced to fit more closely around the substrate</one>.
+- Give an example for <one>a protein</one> with an <two>ATP-dependent protease activity</two>. A: The <one>RecA protein</one>. URL: https://en.wikipedia.org/wiki/RecA
+- Name a <one>major protein structure classification scheme</one>. A: <one>SCOP</one>: <two>Structural Classification of Proteins</two> URL: https://scop.mrc-lmb.cam.ac.uk/
+- <one>Can</one> <two>proteins</two> <one>unfold upon cooling</one>? <one>Yes</one> - this phenomenon is known as <two>cold denaturation</two>.
+- The <one>electrostatic interactions</one> <two>can function within a range of about ... </two>? <one>15 Angstrom</one>.
+- Name <one>a protein</one> consisting largely of beta sheets, starting with the letter <two>p</two>. A: <one>Pepsin</one>. URL: https://en.wikipedia.org/wiki/Pepsin
+- What can be considered to be <one>the building blocks of protein structure</one>? The <one>peptide units</one>.
+- Give <one>two different reasons</one> why we may wish to employ <two>X-ray</two> on protein crystals. A: (1) <one>design novel drugs</one> that target a particular protein (2) rationally engineer an enzyme for a specific industrial process
+- When we <one>compare two different proteins to one another</one>, through <two>percent identity</two>: can the percent identity be <three>zero</three>? <one>No</one> - <two>proteins always have something in common</two>.
+- Ein <one>Hsp70-Molekül</one> bindet an etwa n Aminosäuren? Etwa <one>7 Aminosäuren</one>.
+- Die <one>Peptidbindung</one> <two>absorbiert Licht mit einer Wellenlänge von ... </two>? Von <one>190 nm bis 230 nm</one>.
+- What are <one>Thermosomes</one>? <one>Thermosomes</one>, found in some <two>Archaea</two>, are hollow balls inside which proteins are folded. URL: https://en.wikipedia.org/wiki/Thermosome
+- Nenne <one>zwei</one> <two>3D-Eigenschaften</two> der Peptidbindung. A: (1) <one>Planarität</one> (2) <one>Konformation</one>
+- <one>What happens</one> if we add an increasing amount of <two>Guanidinium chloride</two> to proteins in solution? These <one>proteins will unfold</one>. URL: https://en.wikipedia.org/wiki/Guanidinium_chloride
+- Every protein has <one>a free amino terminus</one> at one end and <one>a free carboxy terminus</one> at the other end, <two>except for ... </two>? A few <one>cyclic polypeptides</one>.
+- <two>Christian Anfinsen</two> worked with <one>which enzyme</one> in particular, <three>in order to demonstrate that proteins can refold</three>? The enzyme <one>ribonuclease</one>.
+- <one>Warum</one> kann die Strukturbiologie kaum auf Einzelebene der Aminosäuren Vorhersagen treffen? Da selbst wenn wir, zum Beispiel, zwei Aminosäuren beschreiben können, die miteinander wechselwirken, wir eine unrealistische Annahme treffen, da ein Protein aus vielen Aminosäuren besteht, die miteinander in 3D sich gegenseitig beeinflussen können (+ Wassermoleküle in der Umgebung).
+- The <one>ATPase</one> contains the <two>F₀ channel</two>, <three>allowing the passage of ... </three>? <one>H⁺</one>.
+- Was wird als <one>Apoprotein</one> bezeichnet? <one>Der Teil eines Proteins</one>, <two>der nur aus Aminosäuren besteht</two>.
+- <one>Wasserstoffbrücken</one> <two>entstehen generell zwischen ...</two>? (1) <one>Wasserstoff</one> und <two>Sauerstoff</two> (<two>O</two>) (2) <one>Wasserstoff</one> und <two>Stickstoff</two> (<two>N</two>)
+- Hat <one>Zink</one> einen <two>Einfluss auf den pKA von Aminosäuren</two>? <one>Ja</one>. <two>Zink</two> bindet die Aminosäuren Histidin und Cystein und <one>senkt dadurch deren pKa</one>.
+- Strictly speaking, from the point of structural biology, the term <one>hydrophobic proteins</one> is misleading. <two>Why</two>? Because it is <one>the water</one> which dislikes the dissolved non-polar groups.
+- <one>Benötigen</one> große Proteine Hilfe von Chaperonen? <one>Ja</one>, <two>eigentlich immer</two>.
+- <one>Fhkl</one> <two>is a mathematical function, used in x-ray crystallography</two> <three>that describes the amplitude and phase of a wave diffracted from crystal lattice planes</three>, characterized by ... indices h,k,l. A: <one>Miller indices</one>.
+- <one>Warum</one> ist <two>die Konformationsänderung von Lactoferrin</two> wichtig? Weil andere Proteine diese Änderung erkennen können.
+- The canonical example to be given for a protein with a quarternary structure is ... ? <one>hemoglobin</one>.
+- Name a <one>hemoglobin-variant</one> that begins with the letter C and was discovered in the year 2001. A: <one>Cytoglobin</one>. URL: https://en.wikipedia.org/wiki/Cytoglobin
+- <one>Cytochrom-c-Proteine</one> <two>besitzen welche Aminosäuren-Signatur</two>, das Erkennungsmotiv dieser Proteingruppe? <one>CXXCH</one>. URL: https://en.wikipedia.org/wiki/Cytochrome_c#Structure
+- Is <one>water</one> <two>part of a molecule</two>, as far as structural biology is concerned? This depends; internally bound water molecules can be regarded as <one>integral parts of the protein structure</one> at hand.
+- A <one>sticky patch</one> <two>on the surface of a molecule can create problems</two>. <three>Give a specific example to reinforce this statement</three>. A: <two>Hemoglobin</two>, in the sickle-cell mutation, has such a <one>sticky patch on the surface</one>. In this mutation, a charged glutamic acid is replaced with the non-polar valine, which causes this <one>sticky patch</one> situation.
+- Der <one>Ionenkanal MscL</one>, <two>ein Mechanosensor im Bakterium Mycobacterium tuberculosis</two>, <three>besteht aus wievielen Untereinheiten</three>? Aus <one>fünf</one> (<two>5</two>).
+- Aus Sicht der Strukturbiologie: <one>wieso</one> wirkt <two>Quecksilber</two> <three>toxisch</three>? Quecksilber kann Enzyme und Proteine destabilisieren, indem es an deren Sulfhydryl-Gruppen bindet.
+- <one>Proteins</one> in general <two>adopt which structure</two>? The structure that <one>minimizes free energy</one>.
+- Nenne <one>drei</one> <two>Kenngrößen der Alpha-Helix</two>. A: (1) <one>Ganghöhe</one> (2) <one>Anstieg</one> (3) <one>Drehung</one>
+- The <one>alpha helix</one> <two>twists around like a</two> ... ? <one>spiral staircase</one>.
+- In <one>structural biology</one>, name <two>the three core aspects</two> to give a <three>comprehensive picture of proteins</three>. A: (1) <one>structure</one> (2) <one>thermodynamics</one> (3) <one>kinetics</one>
+- Molekulargewicht von <one>Myosin II</one>, <two>in kDa</two>? <one>500 kDa</one>. URL: https://de.wikipedia.org/wiki/Myosin_II
+- The <one>unique biochemical fingerprint of proteins</one> is ... ? Their <one>aminoacid sequence</one>.
+- <one>How</one> do we call the <two>small metal disk</two> in the middle of a X-Ray diffraction pattern? <one>Beam stop</one>. URL: https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3150576/
+- <one>Hsp70</one> <two>bindet an ...</two> <three>welche Bereiche eines ungefalteten Proteins</three>? An <one>hydrophobe Segmente</one>. URL: https://en.wikipedia.org/wiki/Hsp70
+- <one>How many</one> <two>protein families</two> were known in the year 2013? At the least <one>14.830</one>.
+- How do we call the <one>independent folding units in a protein</one>? These are the <one>protein domains</one>.
+- The <one>peptide unit length</one> is <two>n Angstrom</two>? About 3.5 Angstrom.
+- <one>Disulfide Bridges</one> <two>can occur in which of two ways</two>? (1) <one>Interchain Disulfide Bridges</one> (2) <one>Intrachain Disulfide Bridges</one> (see also https://www.ncbi.nlm.nih.gov/pmc/articles/PMC389237/) 
+- Nenne <one>zwei Strukturmotive</one>, die <two>beta</two> in ihrem Namen inkludieren. A: (1) <one>beta-Sandwich</one> (2) <one>beta-Barrel</one>
+- The protein GFP contains n beta-strands arranged into a barrel? <one>11</one>.
+- Give an example for a <one>rotary biomolecule</one>. A: The <one>ATPase</one>.
+- Name <one>the two major contributors</one> to the energy difference between <two>the folded state</two> and <two>the denatured state</two>. A: (1) <one>enthalpy</one> (2) <one>entropy</one>
+- <one>How long</one> is a <two>beta sheet</two> typically, in <three>n aminoacids</three>? <one>3-10 aminoacids</one>.
+- Wie sind <one>antiparallele Faltblattstränge</one> verbunden? Durch eine <one>Beta-Schleife</one>.
+- <one>Bei welchem Protein</one> im menschlichen Körper kann der <two>allosterische Effekt</two> sehr gut beobachtet werden? Bei <one>Hämoglobin</one>. URL: https://de.wikipedia.org/wiki/H%C3%A4moglobin
+- A <one>membrane-spanning protein</one>, in its simplest form, has <two>how many and which segments</two>? <one>3</one>. (1) <two>one hydrophobic transmembrane segment</two> (2) <two>two hydrophobic regions</two>
+- Give an entertaining name for an <one>intrinsically unfolded</one> protein. A: A <one>floppy protein</one>.
+- The <one>average length of an alpha-helix</one> is ...? About <one>10 amino acid residues</one>.
+- <one>Welche Proteine</one> besitzen typischerweise <two>Disulfidbrücken</two>? Jene Proteine die das Endoplasmatische Retikulum durchschreiten - also vor allem <one>sekretorische Proteine</one>.
+- What is <one>the basic paradigm of structural biology</one>? <one>Sequence → Structure → Function</one>.
+- Between the <one>unfolded</one> and the <one>folded state</one> of proteins lies <two>which other state</two>? The <one>molten globule</one>. URL: https://de.wikipedia.org/wiki/Molten_Globule
+- Give another name for <one>the fold space</one>. A: <one>Structure space</one>.
+- <one>Polypeptide chains</one> with similar amino acid sequences fold to give ... ? <one>Similar 3D structures</one>.
+- Give an example for <one>a globular, flexible molecule</one> that consists primarily of α-helices. A: <one>Myoglobin</one>. URL: https://en.wikipedia.org/wiki/Myoglobin
+- Die Famile der <one>fork head HNF-3-related genes</one> kodiert für Transkriptionsfaktoren, der sogenannten <two>Fork head Box</two>. Diese Sequenz ist hoch konserviert, und umfasst in etwa wieviele Aminosäuren? Etwa <one>110 Aminosäuren</one>. Dieses Motiv wird mitunter auch <two>Winged-Helix Motiv</two> genannt.
+- Nenne ein Beispiel für eine relativ einfache <one>Supersekundärstruktur</one> in Proteinen. A: <one>Zwei Beta-Faltblätter</one>, die über eine Alpha-Helix miteinander verbunden sind.
+- Ist <one>Hämoglobin</one> ein <two>Homotetramer</two>? Nein. <two>Hämoglobin</two> ist ein <one>Heterotetramer</one>. URL: https://de.wikipedia.org/wiki/H%C3%A4moglobin#Struktur
+- <one>What is responsible</one> for <two>the formation of alpha-helices and beta-sheets</two>? <one>Hydrogen bonding</one>. URL: https://www.britannica.com/science/hydrogen-bonding
+- What happens if we add an increasing amount of <one>GdmCl</one> (<cadetblue>guanidium chloride</cadetblue>) to proteins in solution? These <one>proteins will unfold</one>. URL: https://en.wikipedia.org/wiki/Guanidinium_chloride
+- Proteine wie zum Beispiel das <one>SSB-Protein</one> sind <two>"kooperativ"</two>. Was ist mit dieser Aussage gemeint? Das <one>ein gebundenes SSB-Protein</one> <two>die Bindung weiterer SSB-Proteine erleichtert</two>.
+- Why would a cell require <one>rigid proteins</one>? In theory, <one>such proteins may be more stable</one> - but most proteins need some <two>structural flexibility</two>, so too rigid proteins are not a good idea from this point of view.
+- Name <one>two aminoacids</one> that are <two>effective chelators of metal ions</two>. A: (1) <one>Aspartic acid</one> (<two>aspartate</two>) (2) <one>Glutamic acid</one> (<two>glutamate</two>)
+- Nenne ein konkretes Beispiel für ein Protein das ein <one>four-helix bundle</one> inkludiert. A: <one>Cytochrom b562</one>. URL: https://de.wikipedia.org/wiki/Cytochrom_b
+- Eine <one>Protein-Protein-Interaktion</one> ist <two>eine Wechselwirkung zwischen zwei oder mehreren Proteinen</two>. Sie beruhen überwiegend auf ... ? Auf <one>nicht-kovalenten Wechselwirkungen</one> - wie <two>van-der-Waals-Kräfte</two>, Wasserstoffbrückenbindungen sowie elektrostatischen Wechselwirkungen.
+- In protein folding: <two>which state</two> occurs before the <one>final native state</one> of a folded protein? The <one>molten globule state</one>. URL: https://en.wikipedia.org/wiki/Molten_globule
+- Name the <one>three major advantages</one> of <two>NMR-spectroscopy</two> compared with X‐ray crystallography. A: (1) Protein structures in solution (2) Protein dynamics (3) Some proteins cannot be crystallized
+- Eine Aminosäure nimmt circa welches <one>Volumen</one> ein? <one>5 Angstrom x 5 Angstrom x 5 Angstrom</one>: also <two>125 Kubik-Angstrom</two>.
+- The <one>alpha helix</one> is also called a classic ... ? <one>Pauling-Corey-Branson</one> alpha-helix.
+- Name <one>two aminaocids</one> that show a <two>high propensity to form beat-sheets</two>. A: (1) <one>serine</one>   (<two>S</two>) (2) <one>threonine</one> (<two>T</two>)
+- Wie wird die <one>Bindungsstärke eines Proteins</one> genannt? <one>Affinität</one>.
+- Wenn wir <one>Calcium</one> (<two>²⁺</two>) mit <one>Zinn</one> (²⁺) vergleichen, die beide eine wichtige Rolle in der Strukturbiologie spielen mögen, <two>wer von den beiden besitzt einen kleineren Ionenradius</two>? <one>Zinn</one>.
+- Die <one>Chromodomäne</one>, eine Proteindomäne von etwa 40-50 Aminosäuren Länge, <two>wurde zuerst wo entdeckt</two>? Im <one>Drosophila melanogaster</one> Protein <two>Polycomb</two> (Pc).
+- For <one>crystal structure</one>: we may modify <two>methionine</two> by adding which atom rather than its sulfur? <one>Selenium</one>.
+- Was ist die <one>EF-Hand</one>? In der Proteinchemie, die Abfolge <one>Helix E</one>, <one>loop</one>, <one>Helix F</one>.
+- In amino acids, the <one>carboxyl groups</one> can be coupled to ...? <one>Amines</one>.
+- A <one>single amino acid residue</one> spans ... <two>how many Angstrom</two>, roughly? About <one>3,8 Angstrom</one>.
+- <one>A single amino acid residue</one> <two>spans about how many Angstroms</two>? About <one>3,8 Å</one>.
+- How do we call any region of a <one>protein surface</one> that allows interaction with another protein? A <one>binding site</one>.
+- Which <one>physical force</one> or <one>physical factor</one> is highly responsible for <two>the specificity of interaction</two> between proteins? <one>Hydrogen bonds</one>.
+- Im <one>Ramachandran-Plot</one> finden wir <two>links oben</two> ... ? Die <one>beta-sheets</one>.
+- In the <one>Protein Data Base</one> (<one>PDB</one>), as of the year <two>2017</two>: <three>how many percent of the structures registered there were solved by X-Ray analysis</three>, roughly? Almost <one>90%</one>.
+- The ... of a protein is <one>the really stable form</one>. A: The <one>aggregate</one>.
+- About <one>one third of all proteins</one> are ... ? <one>Metalloproteins</one>.
+- In structural biology we can identify the so-called <one>β-Bends</one>. <two>Why was that name given to them</two>? <one>β-Bends</one> were given this name because <two>they often connect successive strands of antiparallel β-sheets</two>.
+- In structural biology: define the term <one>heteromultimeric</one>. A: These proteins contain <one>two ore more</one> <two>different polypeptide chains</two>.
+- Give an example for a protein consisting predominantly of <one>alpha-helices</one>. A: <one>Myogloblin</one>.
+- <one>When</one> were <two>x-rays</two> discovered? In <one>1901</one>, by <two>W. C. Röntgen</two>.
+- When will a protein <one>NOT</one> have a <two>quaternary structure</two>? When it has <one>only one polypeptide chain</one>.
+- Durchmesser einer <one>Alpha-Helix</one>, <two>in Angstrom</two>? <one>14 Angstrom</one>.
+- In structure determination of proteins: the technique <one>ORD</one> is ... ? <one>Optical rotary dispersion</one>. URL: https://en.wikipedia.org/wiki/Optical_rotatory_dispersion
+- For the <one>phasing of protein crystals</one> in X-ray crystallyography, <two>what is absolutely required</two>? An <one>electron density map</one>.
+- <one>Welche Konformationen</one> kann eine <two>Peptidbindung</two> in einem Protein einnehmen? (1) <one>cis</one> (2) <one>trans</one>
+- Andere Bezeichnung für die <one>Tertiärstruktur der Proteine</one>? <one>Domänen</one>.
+- The <one>proline helix</one> is a <two>left handed</two> or a <two>right handed</two> helix? It is <one>left handed</one>.
+- What is <one>the underlying principle of molecular function</one>? <one>Structure</one>.
+- <two>Beta Sheets</two> can be <one>antiparallel</one> and <one>parallel</one>. Which one of these two is more stable? <one>Antiparallel</one> is <two>more stable</two>.
+- <one>Beta-Barrels</one> can have <two>which three major structures</two>? (1) <one>greek keys</one> (2) <one>jelly rolls</one> (3) <one>up-and-down barrel</one>
+- Die häufigste Form der <one>kovalenten Modifikation</one> von Proteinen ist ... ? Die <one>Phosphorylierung</one>.
+- Der <one>durchschnittliche Stickstoffgehalt von Proteinen</one> beträgt <three>n%</three>? <one>16%</one>.
+- Name a <one>biophysical method</one> with which we could <two>discover protein-protein interaction sites</two>. A: <one>NMR Mapping</one>. URL: https://www.nature.com/articles/nmeth0206-80
+- <one>Asparagine residues</one> are often found <two>where</two> in an <three>alpha-helix</three>? Near the <one>beginning</one> or the <one>end</one> of that alpha-helix.
+- A protein contains <one>internal peptide bonds</one>, which <two>are formed during a condensation reaction</two> - thus, water is formed. <three>Who contributes the atoms in the H₂O molecule</three>? The <one>carboxyl group (COOH)</one> contributes a <two>H</two> and a <two>O</two>, and the amino group loses a N.
+- Give an example for a protein that consists of a <one>beta-barrel</one>. A: The <one>Porin proteins</one>. URL: https://en.wikipedia.org/wiki/Porin_(protein)
+- Name <one>two intrinsic reasons</one> for what may complicate the folding process of proteins. A: (1) disulfide bridge: in particular when non-native disulfide bridges are possible (2) cis-trans isomerization of proline residues
+- Das <one>Ca-Bindungsmotiv</one> wird <two>von welcher Aminosäure bereitgestellt</two>? <one>Aspartat</one> (<two>D</two>).
+- The <one>3.10 helix</one> has <two>n amino acids per turn</two>? <one>3</one>. URL: https://en.wikipedia.org/wiki/310_helix
+- The value of the <one>dielectric constant D</one> is important in structural biology. It has <two>a value of about 80 in water</two>, and ... in the hydrophobic core of a protein. A: About <one>3-5</one> <two>in the hydrophobic core of a protein</two>.
+- <one>Wie</one> konnte man die Bindungslänge und den Bindungswinkel der Peptidbindung bestimmen? Mit Hilfe der <one>Röntgenstrukturanalyse</one>.
+- Je kleiner der <one>KD-Wert</one>, desto ... ist die <one>Affinität</one>? Desto <one>größer</one>/<one>höher</one>.
+- The <one>Protein Structure Continuum</one> may lead to <two>IDPs</two>. What does this abbreviation stand for? <one>IDPs</one> stands for <two>Intrinsically Disordered Proteins</two>. URL: https://en.wikipedia.org/wiki/Intrinsically_disordered_proteins
+- Give an example for <one>a transport protein</one>. A: <one>Hemoglobin</one>. URL: https://en.wikipedia.org/wiki/Hemoglobin
+- Name the <one>three main methods for protein structure determination</one>. A: (1) <one>X-ray Crystallography</one> (2) <one>NMR Spectroscopy</one> (3) <one>Electron Microscopy</one>
+- For structural biology it is useful to remember <one>the molecular mass of the average amino acid</one>, which is ... ? <one>100 Da</one>.
+- A <one>crystal</one> consists of ...? <one>Identical unit cells</one>. URL: https://en.wikipedia.org/wiki/Crystal
+- In structural biology: is the <one>left handed helix</one> more common than the <one>right handed helix</one>? <two>No</two> - <one>the right handed helix is more common</one>.
+- Das <one>Beta-Haarnadelschleifenmotif</one>: <two>nenne ein Beispiel eines Proteins, das dieses Motif besitzt</two>. A: <one>Bovine Trypsin Inhibitor</one>.
+- Im <one>Ramachandran-Plot</one> finden wir <two>links unten</two> ... ? Die <one>Alpha-Helix</one>. URL: https://de.wikipedia.org/wiki/Ramachandran-Plot
+- If we are to <one>increase the negative surface charge</one>, would this <two>affect protein solubility</two>? If so, how? A: An increase in the negative surface charge correlates strongly with <one>increased protein solubility</one>.
+- Say that a researcher employs <one>Dithiothreitol</one>. <two>What will the effect be upon proteins</two>? <one>Dithiothreitol</one> is a <two>thiol reagent</two> that <three>will dissolve disulfide bonds</three> between cysteine amino acids.
+- Can the <one>peptide bond</one> be involved in <two>hydrogen bonds</two>? Yes. See the stabilization in <one>α-helices</one> and in <one>β-sheets</one>.
+- <one>The first resolved crystal structure of a protein</one> was <two>hemoglobin</two>, in the year ... ? <one>1959</one>. URL: https://en.wikipedia.org/wiki/Hemoglobin
+- Das <one>BiP</one> (<two>Binding Protein</two>) ist <three>worin</three> eine Schlüsselkomponente? <one>BiP</one> ist eine Schlüsselkomponente in der <two>Unfolded protein response</two>. URL: https://en.wikipedia.org/wiki/Unfolded_protein_response
+- Verschiedene Aminosäuren haben eine <one>unterschiedliche Neigung</one> zur <two>Alpha-Helix Strukturbildung</two>. <three>Welche fünf Aminosäuren sind besonders gute Alpha-Helix Strukturbildner</three>? <one>MALEK</one> (1) <two>Methionin</two> (2) <two>Alanin</two> (3) <two>Leucin</two> (4) <two>Glutamat</two> (5) <two>Lysine</two>
+- Compare <one>the average length of soluble proteins</one> to <two>membrane-bound proteins</two>. A: <one>Soluble proteins</one> <two>tend to be shorter</two> than <one>membrane-bound proteins</one>.
+- <one>Until which year</one> was it not possible to deduce the 3D structure of a large protein? Until <one>1960</one>.
+- Das <one>26S-Proteasom</one> ist ein Proteinkomplex, der <two>wie groß</two> ist (in kDa)? <one>1.700 kDa</one> (=<two>26S-Proteasom</two>).
+- Das <one>Experiment von Anfinsen</one>, 1973, war in der Biochemie sehr wichtig. Als Substrat wurde <two>RNase A</two> verwendet. Was konnte man dank dieses Experiments zeigen? Die <one>RNase A</one> konnte durch <two>Urea</two> und <two>β-Mercaptoethanol</two> denaturiert werden. Danach auch wieder renaturiert, und die volle katalytische Aktivität wurde wieder gewonnen. Das Experiment war wichtig da man zeigen konnte, das die Information für die katalytische Tätigkeit alleine in der Abfolge der Aminosäuren begründet liegt. Zudem demonstrierte man damit auch die Wichtigkeit von <one>spontaneous folding</one>.
+- Give another description for the <one>molten globule</one>. A: The <one>partially structured state</one>. URL: https://en.wikipedia.org/wiki/Molten_globule
+- Preparing a sample for protein analysis via <one>imidazole</one> is difficult, as <one>imidazole</one> can overwhelm the spectrum <two>below ... which nm wavelength</two>? <one>220 nm</one>.
+- <one>Proteins may have stretches of disorder</one>, in their 3D shape. Compare eukaryotes to prokaryotes here: <two>who of these two groups has more disorder in their proteins</two>, in general? <one>Eukaryotic proteins show more disorder</one>. This may be due to the consequence of an increased need for cell signaling and regulation.
+- Nenne drei Vorteile der <one>CD-Spektroskopie</one> (<one>Circulardichroismus</one>) gegenüber der <two>NMR</two>. A: (1) die <one>CD-Spektroskopie benötigt weniger Probenmaterial</one> (2) die <one>CD-Spektroskopie ist schneller</one> (3) die <one>CD-Spektroskopie ist weniger arbeitsintensiv</one>
+- Give an example for <one>a supersecondary (supercoiled) structure in the human body</one>. A: <one>Collagen</one>. URL: https://en.wikipedia.org/wiki/Collagen
+- Which of the following properties of a protein is <one>the least likely</one> to be affected by changes in pH? Pick one from: <two>Secondary structure</two>, <two>Net charge</two>, <two>Primary structure</two> or <two>Tertiary structure</two>. A: <one>Primary structure</one>.
+- Name a protein that is known to form, or be involved in, inter-species, <one>nano-wire</one>-like connections up to 1000 nm. A: <one>Cytochrome c</one>.
+- <one>Lysine</one> has <two>how many different rotamers</two>? <one>81</one> (<two>3⁴</two>).
+- One of the fastest proteins in regards to its own folding is ... ? <one>Ubiquitin</one>. URL: https://de.wikipedia.org/wiki/Ubiquitin
+- <two>Wann</two> wurde das <one>Friedel law</one> etabliert? Im Jahre <one>1913</one>.
+- <one>Ganghöhe</one> der Alpha-Helix? Die Alpha-Helix besitzt eine Ganghöhe von <one>0.54 nm</one>.
+- Warum ist der <one>Hydropathy-Index</one> wichtig? Weil man damit Vorhersagen kann <lightgreen>wo</lightgreen> eine Aminosäure zu finden ist. In einem Protein sind <one>hydrophobe Aminosäuren</one> meistens innen vorzufinden, <one>hydrophile Aminosäuren</one> sind aussen.
+- <one>When</one> was the <two>Levinthal's paradox</two> suggested? In <one>1969</one>. URL: https://en.wikipedia.org/wiki/Levinthal%27s_paradox
+- If we see <one>a protein with a SH2 domain</one>, what can we assume about that protein? That <one>this protein can bind to phosphotyrosines</one>.
+- What is meant with the term <one>protein space</one>? This refers to <one>all possible proteins</one> - <two>an infinite space for the chemical space</two>, which is at the very least larger than protein space.
+- Name a <one>competitive inhibitor</one> that can <two>inhibit many serine proteases</two>. A: <one>Aprotinin</one>. URL: https://en.wikipedia.org/wiki/Aprotinin
+- <two>How many proteins</two>, that is, <one>individual protein molecules</one>, can we find in an average mammalian cell? About <one>10 billion individual proteins</one>.
+- <one>Dr. Michael Rossmann</one> is famous in <two>structural biology</two> for ...? Discovering the <one>Rossmann fold</one>. URL: https://en.wikipedia.org/wiki/Rossmann_fold
+- Give another term for <one>angle pairs</one> of <two>phi</two> and <two>psi</two> in structural biology. A: <one>Ramachandran plot</one>.
+- Ändert <one>Calmodulin</one> seine 3D-Struktur wenn es <mediumturquoise>Calmodulin</mediumturquoise> gebunden hat? Ja. URL: https://de.wikipedia.org/wiki/Calmodulin
+- <one>CD-Spektroskopie</one>: wofür steht hier die Abkürzung <one>CD</one>? <one>Circulardichroismus</one>. URL: https://de.wikipedia.org/wiki/Circulardichroismus
+- <one>Natural proteins fold spontaneously</one> to form unique, native structures. <two>How can this work</two>? The polypeptide chain is flexible. This allows these proteins to assume many different spatial conformations. At equilibrium the protein will adopt the native state.
+- Why can we not use <one>imidazole</one> in <two>protein spectroscopy</two>? Because <one>imidazole overwhelms the spectrum from then on</one>.
+- <two>Wo</two> (in einem Protein) findet man <one>phosphorylation sites</one>? Auf der <one>Oberfläche eines Proteins</one>.
+- <two>Welche Person</two> schlug das <one>ribbon-Modell</one> für Proteine vor? <one>Jane Richardson</one>. URL: https://en.wikipedia.org/wiki/Jane_S._Richardson
+- In order to <two>crystallize</two> <one>problematic proteins</one>, <three>what kind of optimization</three> may we have to do in the lab usually? <one>Buffer optimization</one>.
+- Die <one>relative Molekülmasse</one> eines Proteins (Mr) ist ... ? <one>38.000</one>.
+- <two>Where</two> in the Ramachandran Plot can we find <one>left handed alpha-helices</one>? In the <one>upper right quadrant</one>. URL: https://en.wikipedia.org/wiki/Ramachandran_plot
+- Ein typisches <one>Beta-Faltblatt</one> enthält (von-bis) Beta-Stränge? Ein typisches Beta-Faltblatt besteht aus <one>2-15</one> einzelnen Beta-Strängen.
+- If we have <one>an insoluble protein</one>, what could we do in the laboratory to make it more soluble? We could <one>attach SUMO to it</one>. <two>Ubiquitin-like proteins tend to fold very quickly in general</two>.
+- Give the mnemonic for <one>the trend of hydrophobicity parameters</one> for the L-aminoacids. A: F,(L,I),(Y,W),V,M,P,C,A,G,T,S,K,Q,N,H,D,E,R. Also, Phenomenäle Läuse der Isolde Yagen wilden Valentin.
+- Name one big advantage that <one>X-Ray</one> has over <one>NMR</one>. A: <one>X-Ray has no size limitation</one> in regards to the structure to be studied.
+- The <one>ends of alpha helices</one> can be found <two>where in a protein</two>? The <one>ends are</one> <two>polar</two>, and thus almost always on the <one>surface of protein molecules</one>.
+- Give a specific example for a protein that consists of lots of <one>alpha-helices</one>. A: <one>Myoglobin</one>. URL: https://en.wikipedia.org/wiki/Myoglobin
+- Name <one>an important reason</one> as to why we <two>attempt to determine protein structures through high-throughput methods</two>. A: <one>Lower cost</one> due to <two>automation</two>.
+- <one>NMR analysis</one> works up to a protein size of n Daltons? Up to <one>100.000 Daltons</one>.
+- If we conclude that <one>two proteins are homologouos</one>, what else can we conclude from that statement, if it is true? That <one>their genes</one> must have evolved from a <two>common ancestral gene</two>.
+- In structural biology: in general the <one>X-ray method</one> is much better than the <one>NMR method</one>. One difficulty is to obtain the crystals, but <two>name an area where the NMR in particular excels</two>. A: <one>NMR</one> can be used to study <two>protein dynamics</two>.
+- Give <one>seven general examples</one>/<one>reasons</one> as to the different functions of proteins. A: (1) structural proteins (2) enzymes (3) antibodies (4) regulatory proteins (5) sensors (6) <one>transporters</one> (7) <one>transducers</one>
+- In the <one>core</one> of <two>a typical globular protein</two>: <three>which factor is the most important one that stabilizes the core</three>? The <one>van-der-Waals force</one>.
+- <one>Tryptophan</one> is often found where exactly on a given protein? <one>In the core</one> (aka center), primarily <two>due to its bulky shape</two> and secondarily due to its hydrophobicity.
+- <one>Wann</one> wurde die <two>Struktur von Lysozym</two> aufgeklärt? Im Jahre <one>1965</one>. URL: https://de.wikipedia.org/wiki/Lysozym#Geschichte
+- Nenne ein sehr häufiges Protein, das weitgehend aus <one>Alpha-Helices</one> besteht. A: <one>Hämoglobin</one>. URL: https://en.wikipedia.org/wiki/Alpha_helix#Functional_roles
+- <one>Wovon</one> ist das Auflösungsvermögen einer <two>Röntgenanalyse</two> primär abhängig? Von der <one>Qualität des Kristalls</one>.
+- Was meinen wir mit <one>exozyklisch</one>? Dies ist <one>nicht im Ring</one>, zum Beispiel bei RNA, das C5'-Atom.
+- The <one>helix-turn-helix motif</one> is a functional motif that is often found in proteins that bind to DNA minor and major grooves, as well as proteins that <two>bind which metal</two>? <one>Calcium</one> - thus, in <two>calcium-binding proteins</two>.
+- What does the <one>Anfinsen dogma</one> state? <one>Protein folding occurs in self-assembly</one>. In other words, the peptide sequence contains the whole information for its assembly.
+- A <one>FRET signal</one> provides information about distances in the order of ... Å? About <one>10 Å to 100 Å</one>.
+- Anderer Begriff für <one>Tertiärstrukturen</one>? Möglicher <one>Endzustand eines Proteins</one>.
+- Wenn ein <one>Anion</one> in einem Protein stabiler wird, <two>wie ändert sich die Säurestärke</two>? Die <one>Säurestärke steigt</one>.
+- Welche <one>drei Komponenten</one> werden für eine <two>röntgenkristallographische Analyse</two> benötigt? (1) einen <one>Detektor</one> (2) ein <one>Proteinkristall</one> (3) <one>eine Quelle für Röntgenstrahlen</one>
+- Nenne <one>die drei wichtigsten Sekundärstrukturelemente von Proteinen</one>. A: (1) <one>alpha-Helix</one> (2) <one>beta-Faltblatt</one> (3) <one>beta-Schleife</one>
+- In general: what is meant with <one>the hydrophobic effect</one>? The hydrophobic effect generally refers to the low solubility of hydrophobic compounds in water. These are <one>apolar</one> compounds. 
+- The rarer a protein-coding variant is (for a given gene), the more likely it is to represent ... what kind of change? a <one>non-conservative amino acid change</one>.
+- Name <one>two functionally important areas of proteins</one> in general. A: (1) <one>ligand-binding   sites</one> (2) <one>enzymatic active sites</one>
+- Können wir aus <one>Proteinstrukturen</one> auf <two>Liganden</two> ableiten? Ja, zum Teil: <one>Ähnliche Proteinstrukturen</one> bedeuten oft <two>ähnliche Liganden</two>.
+- Give an example of <one>where</one> we can find the <two>greek key motif</two>, a protein example. A: In the <one>Staphylococcus nuclease</one>. URL: https://en.wikipedia.org/wiki/Greek_key
+- We have the <one>Nm nomenclature for helices</one>. What does the <two>N</two> stand for, here? <two>N</two> refers to the <one>number of repeating units per turn</one>.
+- Is the <one>amide linkage</one> (of the peptide bond) <two>important for protein stability</two>? Yes. The amide linkage is very important for the three-dimensional structure of peptides and proteins.
+- <one>Proteine variieren sehr stark in der Größe</one>, <two>von nDa bis zu nDa</two>? Von <one>5_000 Da</one> bis zu <one>3_000_000 Da</one>.
+- How do we call <one>folding possibilities</one> of proteins? The <one>conformation space</one>.
+- What is <one>the major unsolved problem</one> in <two>structural molecular biology</two>? How to <one>predict the three-dimensional structure of a protein</one>.
+- How are <one>regions of a protein</one> called that do not form a secondary structure? A <one>random coil</one>.
+- In general, <one>where</one> do <two>Beta-Hairpin turns</two> occur? They occur between <one>two antiparallel beta-strands</one>.
+- A <one>chaperone</one> generally binds to ..? A <one>partly folded polypeptide chain</one>.
+- <one>PDB</one> contains a lot of proteins. How many in the year <two>2016</two>? About <one>67.700</one>.
+- Name a <one>major advantage of NMR-spectroscopy</one> compared to <two>X-ray crystallography</two>. A: We can <one>study protein structures in solution</one>.
+- The <one>folding process</one> goes from a high energy unfolded state to a low energy native state, through ... states. A: <one>metastable intermediate states</one>.
+- <one>Starke Helix-Brecher</one> sind zum Beispiel <two>Glycin</two> oder <two>Prolin</two>. Es gibt jedoch auch zwei schwache Helix-Brecher, ebenso Aminosäuren. Welche zwei sind dies? (1) <one>Asparagin</one> (2) <one>Tyrosin</one>
+- The <two>intrinsic factors</two> that influence <one>protein solubility</one> are defined primarily by ... ? By the amino acids on the protein surface.
+- For <one>a general classification scheme</one>: which <two>three types of proteins exist</two>? (1) <one>structural proteins</one> (2) <one>membrane proteins</one> (3) <one>globular proteins</one>
+- Erreichbare Auflösung bei der <one>Einzelkristallröntgenbeugung</one>? <one>1 Angstrom</one>.
+- In der Strukturbiologie: was meinen wir mit <one>MAD</one>? <one>Multi-wavelength anomalous diffusion</one>.
+- Wieso ist <one>die globuläre Kugelform bei Proteinen</one> so häufig zu sehen? Dies ist <one>eine Konsequenz des hydrophoben Effekts</one>.
+- Was ist bei der Verwendung eines <one>Protease-Inhibitor Cocktails</one> zu beachten? <two>Zellen enthalten verschiedene Proteasen, die Proteine unspezifisch degradieren mögen</two>. Organellen können zerstört werden und so auch ihre spezifischen Proteasen freisetzen. Man sollte <one>nur soviel Inhibitoren hinzufügen, um die Proteolyse, die man verhindern möchte, aufzuhalten</one>.
+- Which <one>direction</one> (left-handed versus right-handed) is <two>FORBIDDEN</two> for an alpha-helix formed by L-amino acids? A <one>left-handed alpha-helix</one> is not allowed for the <two>L-amino acids</two>.
+- The <one>alpha helix</one> is also known as the <two>3.613-helix</two>. What does the 13 indicate here? <one>13 atoms</one> are involved in the ring formed by the hydrogen bond.
+- What are <one>molten globules</one>? <two>Molten globules</two> are compact, <one>partially folded conformations</one> of proteins that have near-native compactness.
+- Do <one>cis-peptide bonds</one> exist in nature? Yes, in <two>cyclic dipeptides</two> for example, as can be found in the <two>diketopiperazines</two>. URL: https://en.wikipedia.org/wiki/Diketopiperazine
+- In structural biology: what is meant with the <one>hydrophobic effect</one>? These are mostly the hydrophobic sidechains in the interior of a protein (or a protein structure).
+- Why is the <one>N-terminal part</one> of the <three>lactate dehydrogenase</three> important? Because it will interact with other subunits, thus keeping the whole complex together.
+- Einfaches Merkschema (Mnemonic) für das <one>Greek key motife</one>? <one>rauf-runter-rauf-runter</one>.
+- Es gibt das <one>CATH protein structure classification</one>. Wofür steht die Abkürzung <two>CATH</two>? (1) <one>Class</one> (2) <one>Architecture</one> (3) <one>Topology</one> (4) <one>Homology</one>
+- One strategy used to design a stronger, better alpha-helix is via <one>capping</one>, in particular ... ? <one>N-capping via Asparagin</one>.
+- Eine <one>Peptidbindung</one> ist eine ... Bindung zwischen der Carboxygruppe einer Aminosäure und der Aminogruppe des α-Kohlenstoffatoms einer zweiten Aminosäure. A: Eine <one>amidartige Bindung</one>.
+- Name a program for <one>Peptide helicity prediction</one>. A: <one>AGADIR</one>.
+- Allgemein gilt bei <one>Glycin</one> was in einem Protein? Glycin findet sich oft an Positionen in der Peptidkette, die sich bewegen oder eine Art <one>Gelenk des Proteins</one> darstellen.
+- What is meant with the term <one>hydrophobicity profile</one>? This is when we use a hydrophobicity scale that assigns a value to each amino acid, and to then plot the variation of hydrophobicity along the sequence of the protein.
+- <one>Carbon-carbon bond distance</one>, in Angstrom? <one>1.5 Angstrom</one>.
+- <one>Domain swapping</one> is a structural phenomenon that plays an important role in the mechanism of ... of some proteins. A: <one>Oligomerization of some proteins</one>.
+- Nenne ein Beispiel für Proteine, die <one>amphiphile Bereiche</one> besitzen. A: Die <one>Apolipoproteine</one>.
+- What is the biggest problem in <one>X-ray crystallography</one> itself, aside from the difficulty of creating a pure protein crystal? An <one>inability to measure phases directly</one>.
+- Say something about the <one>concentration</one> of hemoglobin in <lightseagreen>red blood cells</lightseagreen>. A: It is <one>almost as high as in the crystalline state</one>.
+- What is <one>apomyoglobin</one>? This is myoglobin without the <one>heme prosthetic group</one>. URL: https://en.wiktionary.org/wiki/apomyoglobin
+- In regards to structural biology: what did <one>Levinthal</one> point out? That proteins cannot fold by random search in <one>conformation space</one>.
+- In X-ray protein research: what is meant with the term <one>model building</one>? This is the process where the electron density map is <one>interpreted in terms of a set of atomic coordinates</one>.
+- The <one>strength of a hydrophobic interaction</one> is proportional to ... ? The surface area that is hidden from water.
+- Nenne einen <one>häufigen Reflex</one> von Proteinen. A: Die Bindung eines Liganden induziert im Protein eine <one>Konformationsänderung</one>.
+- What is the main implication derived from the existence of the <one>Levinthal Paradox</one>? That proteins have evolved <one>mechanisms of efficient folding</one>.
+- Was ist das <one>Friedel law</one>? Eine Eigenschaft von Fourier Transformationen von reellen Funktionen.
+- Nenne <one>ein Beispiel</one> für ein bestimmtes Protein mit einer <two>MBD-Domäne</two>. A: Das <one>MeCP2-Protein</one> besitzt eine <two>MBD Domäne</two>. URL: https://en.wikipedia.org/wiki/MECP2
+- Do <one>alpha-helices</one> have a <two>dipole</two>? <one>Yes</one>.
+- <one>Alpha-Helices</one> contain <two>n amino acids per turn</two>, by default? <one>3.6</one>
+- How do we call <one>identical units</one> in a polypeptide chain? <one>Protomers</one>. URL: https://en.wikipedia.org/wiki/Protomer
+- <one>Proteins are involved in cellular identity</one>. <two>Which proteins in particular</two>? The <one>glycoproteins</one>.
+- A <one>Ramachandran plot</one> <two>will display all aminoacids</two>? <one>No</one> - <two>two aminoacids can not be found there</two>, namely <three>glycine</three> and <three>proline</three> <four>can not be found in a Ramachandran plot</four>.
+- <one>Andere Bezeichnung für</one> <two>fertig gefaltete Untereinheiten</two>? <one>Protomere</one>. URL: https://www.pschyrembel.de/Protomer/H008U
+- Is it easy to <one>refold insulin</one>? <one>No</one>.
+- <two>Wann</two> wurde die <one>Alpha-Helix</one> vorgeschlagen? Im Jahre <one>1951</one>. URL: https://en.wikipedia.org/wiki/Alpha_helix#Discovery
+- The energy of (electrostatic) interaction is described by <one>which law</one>? By the <one>law of Coulomb</one>. URL: https://en.wikipedia.org/wiki/Coulomb%27s_law
+- Give another name for the <one>superfamily of protein kinases</one>. A: The <one>kinome</one>. URL: https://en.wikipedia.org/wiki/Kinome
+- Proteins may show <one>a structure-... relationship</one>. A: A <one>structure-function relationship</one>.
+- Die <one>2D-Kristallisation von Proteinen</one> <two>ist besonders günstig für ... </two>? <one>Membranproteine</one>.
+- <one>Valine</one> <two>stiffens a main polypeptide chain</two> <three>similar to ...</three>? <one>Isoleucine</one>. URL: https://en.wikipedia.org/wiki/Isoleucine
+- Die <one>Alpha-Helix</one> <two>wurde in welchem Jahr postuliert</two>? <one>1951</one>. URL: https://de.wikipedia.org/wiki/%CE%91-Helix#Geschichte
+- Was für ein <one>Profil</one> haben Proteine? Ein <one>Oberflächenprofil</one>.
+- Give <one>an example</one> for a <two>protein</two> that is able to form an <three>infectious conformational state</three>. A: <one>Prions</one>. URL: https://en.wikipedia.org/wiki/Prion
+- Kann <one>Zink</one> den <two>Schwefel von Methionin</two> an sich binden? <one>Ja</one>.
+- Weisen <one>Beta-Faltblätter</one> eine <two>Polarität</two> auf? <one>Nein</one>. URL: https://de.wikipedia.org/wiki/%CE%92-Faltblatt
+- Die <one>2D-Kristallisation von Proteinen</one> erfolgt <two>besonders gut bei welchen Proteinen</two>? Bei <one>Membranproteine</one>.
+- <one>Leucine zipper motifs</one> <two>contain how many alpha helices</two>? <one>Two</one>.
+- <one>Membrane proteins</one> typically - <two>at the least in eukaryotes</two> - <three>constitute n% of proteins encoded by whole genomes</three>? About <one>~30% of proteins</one>.
+- In der schematischen Darstellung der <one>Beta-Stränge</one> <two>zeigen die Pfeilenden worauf</two>? Auf das <one>carboxyterminale Ende</one>.
+- Was kann die <one>EF-Hand</one> <two>binden</two>? <one>Ca²⁺</one>. URL: https://en.wikipedia.org/wiki/EF_hand
+- Can <one>circular dichroism</one> be used to <two>study protein interactions</two>? <one>Yes</one>.
+- Können <one>Ribosomen</one> <two>Chaperonfunktionen</two> besitzen? <one>Ja</one>, <two>zumindest Teile des Ribosoms</two> - diese könnten quasi-Chaperonfunktion besitzen.
+- In <one>Ferritin</one> sind <two>wie viel Prozent der Aminosäurereste</two> zu <three>Alpha-Helices</three> gewunden? <one>75%</one>. URL: https://de.wikipedia.org/wiki/Ferritin
+- Ist <one>für die Synthese einer Peptidbindung</one> ein <two>hoher Energieaufwand</two> <three>notwendig</three>? <one>Ja</one>.
+- Name <one>a substance</one> that <two>can be used to disrupt disulfide bonds of a protein</two>. A: <one>β-mercaptoethanol</one>.
+- The <one>hydrophobic forces responsible for maintaining the 3D structures of proteins</one> <two>can be disrupted by ...</two> what <three>kind of agents</three>? By <one>chaotropic agents</one>. URL: https://en.wikipedia.org/wiki/Chaotropic_agent
+- Ist der <one>Ionenradius</one> von <two>Kalium</two> größer als der von <two>Calcium</two>? <one>Ja</one>.
+- Besitzt das <one>GFP-Protein</one> <two>beta-barrels</two>? <one>Ja</one>.
+- Can <one>a single aminoacid mutation</one> <two>in the core of a protein</two> <three>cause the whole protein</three> to <four>unfold</four>? <one>Yes</one>.
+- In <one>X-ray crystallography</one>: what kind of <two>maps</two> are generated here? In X-ray crystallography <one>electron density maps</one> are generated. URL: https://dictionary.iucr.org/Electron_density_map
+- <one>Chaperone</one> gehören zu welcher <two>Proteinfamilie</two>? <two>Chaperone</two> gehören zu den <one>Hitzeschockproteinen</one>. URL: https://de.wikipedia.org/wiki/Chaperon_(Protein)
+- Say that <one>we want to disorder proteins by changing just one amino acid only</one>. <two>Which amino acid should we choose for this</two>? <two>Cysteine</two>. <two>Cysteine</two> is crucial, as it has a significant contribution to the protein conformation stability via <one>disulfide bond formation</one>. It also is involved in coordination of different prosthetic groups.
+- In einem <one>Ramachandran-Diagramm</one>: <two>wo</two> finden wir das <three>Beta-Faltblatt</three> allgemein eher? <one>Beta-Faltblätter</one> sind eher <two>links oben</two> im Ramachandran-Diagramm vorzufinden.
+- Die <one>Beta-Faltblattstrukturen</one> <two>in globulären Proteinen</two> sind <three>rechtsgängig oder linksgängig</three>? Sie sind <one>ausnahmslos rechtsgängig</one>.
+- Können <one>gasförmige Moleküle</one> <two>Liganden für Proteine</two> sein? <one>Ja</one>.
+- In den <one>Zink-Finger Proteinen</one> (= Transkriptionsfaktoren) wird <two>Zn</two><three>²⁺</three> durch <four>n Cysteine</four> komplexiert? <one>Vier</one> (<two>4</two>).
+- If a <one>flavoprotein</one> appears yellow in colour, <two>what can we subsequently infer from this observation</two>? That this flavoprotein must be in an <one>oxidized state</one>.
+- Wer oder was bestimmt die <one>Halbwertszeit eines Proteins</one>? Die <one>N-terminale Aminosäure</one>.
+- Ist eine <one>Transmembrandomäne</one> eher <two>hydrophil</two> oder eher <two>hydrophob</two>? <one>Transmembrandomänen</one> sind <two>eher hydrophob</two>.
+- What is <one>more stable</one>: <two>parallel</two> or <two>anti-parallel</two> Beta sheets? <one>Anti-parallel Beta sheets</one> <two>are more stable</two>.
+- Wirken <one>chaotrope Substanzen</one> <two>denaturierend</two> <three>auf Proteine</three>? <one>Ja</one>. URL: https://de.wikipedia.org/wiki/Chaotrope_Verbindung
+- Does the <one>F1 ATPase</one> also <two>work in reverse</two>? <one>Yes</one> - <two>the ATPase can work in reverse</two> as well.
+- Does <one>the peptide bond</one> <two>make proteins more resistant to hydrolysis</two>? <one>Yes</one>. Specifically the resonance structure that contributes to the planarity of peptide bonds makes these bonds more resistant to hydrolysis, and thus also the corresponding proteins.
+- Proteine bestehen aus Polypeptiden die eine <one>main chain</one> haben. <two>Verwende ein anderes Wort hierzu</two>. A: <one>Backbone</one>.
+- Es gibt das Strukturmotiv <one>EF-Hand</one>, das man als eine menschliche Hand zeichnen mag. <two>Wieviele Finger müssen wir hierbei verwenden</two>? <one>3</one>. URL: https://en.wikipedia.org/wiki/EF_hand
+- Give an <one>alternative name</one> for <two>non-oligomeres</two>. A: <one>Monomers</one>.
+- Do <one>eukyaryotic proteins</one> <two>get folded inside of the ER lumen</two>? <one>Yes</one>.
+- Warum das <one>Beta</one> in <two>Beta-Faltblatt</two>? Da die <one>Alpha-Helix</one> zuerst gefunden wurde; so erschien es logisch das man Beta einfach Beta nennt.
+- <one>Deutsche Bezeichnung</one> für die <two>X-ray white radiation</two>? Dies bezeichnet die <one>Bremsstrahlung</one>. URL: https://de.wikipedia.org/wiki/Bremsstrahlung
+- Mitglieder eines <one>Beta-Faltblatt</one> heißen (deutsche Bezeichnung) ... ? A: <one>Beta-Stränge</one>.
+- Name <one>a group of proteins</one> that <two>help other proteins fold correctly</two>. A: The <one>chaperone proteins</one>. URL: https://en.wikipedia.org/wiki/Chaperone_(protein)
+- <one>Which aminoacid</one> is <two>a fairly infrequently substituted residue</two>? <one>Cysteine</one>. Often <two>substitution of cysteine with other residues abolishes the enzymatic activity</two>, or destabilizes the protein structure, which may have a similar effect.
+- Die <one>dreidimensionale Faltung der Proteine</one> folgt den <two>Gesetzen der ...</two>? <one>Thermodynamik</one>.
+- <one>Proteins have a ...</one> <two>landscape</two>. A: <one>Proteins</one> have an <two>energy landscape</two>.
+- Are <one>transcription factors</one> <two>more likely to bind to the major groove in DNA</two> <three>than</three> <four>to the minor groove in DNA</four>? <one>Yes</one> - <two>most proteins that interact specifically with DNA bind in the major groove, where space is abundant</two>.
+- Die <one>Carbo-Anhydrase</one> <two>verwendet welches Metall</two>? <one>Zn</one><two>²⁺</two>. URL: https://en.wikipedia.org/wiki/Carbonic_anhydrase
+- Is <one>geometry</one> important for <two>hydrogen bonds</two>? <one>Yes</one>.
+- Wie werden Proteine genannt, die aus <one>mindestens zwei Polypeptidketten</one> bestehen? <one>Multimere Proteine</one>.
+- Does <one>protein folding</one> occur <two>spontaneously</two>? <one>Yes</one>. URL: https://en.wikipedia.org/wiki/Protein_folding
+- Are <one>aminoacids</one> <two>anisotropic compounds</two>? <one>Yes</one>.
+- Die <one>durchschnittliche Proteingröße</one> liegt bei (<two>von-bis</two>) Aminosäuren? <one>200-400</one>.
+- <one>GFP</one> is <two>the representative of which new protein fold</two>? The <one>beta-can</one>. URL: https://www.cryst.bbk.ac.uk/PPS2/projects/jonda/structur.htm
+- <one>Misfolded proteins</one> <two>tend to form ... </two>? <one>Aggregates</one>.
+- <one>Pro ATP</one> rotiert die <two>ATP-Synthase</two> <three>n°</three>? <one>120°</one>. URL: https://de.wikipedia.org/wiki/ATP-Synthase
+- Haemogoblin <one>Hbf</one> ... <two>why</two> the <three>f</three> there? <one>f ... fetal</one>.
+- In einem Protein: <one>parallele Stränge</one> <two>benötigen was</two>? Eine <one>Überkreuzverbindung</one>.
+- Welche <one>drei Möglichkeiten</one> haben <two>Beta-Faltblätter</two> <three>um geordnet zu werden</three>? A: (1) <one>parallel</one> (2) <one>antiparallel</one> (3) <one>gemischt</one>
+- Is <one>the analysis of charge and hydropathy</one> <two>sufficient to distinguish between structured and disordered proteins</two>? In principle <one>yes</one>.
+- Can <one>X-rays</one> <two>be focused by lenses</two>? <one>No</one>.
+- <one>The raw material of proteins</one> <two>is</two>/<two>are ... </two>? <one>Amino acids</one>.
+- Does <one>Ubiquitin</one> have <two>a highly hydrophobic core</two>? <one>Yes</one>.
+- <one>Proteins modified with lipids</one> <two>are termed ... </two>? <one>Lipoproteins</one>. URL: https://en.wikipedia.org/wiki/Lipoprotein
+- Nenne eine (für den Menschen) sehr wichtige Proteingruppe (ausgenommen Insulin), die <one>Disulfidbrücken</one> enthält. A: Die <one>Antikörper</one>.
+- Welche <one>Aminosäure</one> ist meistens bei einer <two>cis-Konformation der Peptidbindung</two> zu finden? <one>Prolin</one>.
+- Kann der <one>Schwefel</one> <two>in einem Zinkfinger</two> <three>chiral sein</three>? <one>Ja</one>.
+- Können <one>CD-Spektren</one> verwendet werden um <two>Cyclopeptide</two> <three>voneinander zu unterscheiden</three>? <one>Ja</one>.
+- <one>Woraus</one> wird <two>die Tertiärstruktur von Proteinen</two> gebildet? Aus <one>Domänen</one>.
+- Does <one>the hydrophobic effect</one> <two>like to mix with water</two>? <one>No</one>, of course not.
+- Wie kann man, einfach und effizient, <two>experimentell feststellen</two>, <one>ob ein Protein in Lösung gefaltet vorliegt</one>? Mit Hilfe der <one>CD-Spektroskopie</one>. URL: https://de.wikipedia.org/wiki/Circulardichroismus
+- Are <one>molten globules</one> <two>more accessible to proteolysis</two>? <one>Yes</one>.
+- <one>Protein space</one> <two>lies within ... </two>? <one>Chemical space</one>. URL: https://en.wikipedia.org/wiki/Chemical_space
+- Andere Bezeichnung für <one>Torsionswinkel</one>? <one>Diederwinkel</one>. URL: https://de.wikipedia.org/wiki/Diederwinkel
+- Do <one>zink finger proteins</one> typically <two>require zink in order to fold</two>? <one>Yes</one> - normally this is the case.
+- In der Strukturbiologie: wofür steht <one>die Abkürzung</one> <two>SCOP</two>? <one>Structural classification of proteins</one>. URL: https://en.wikipedia.org/wiki/Structural_Classification_of_Proteins_database
+- <one>Knowledge of structure</one> is also <two>knowledge of ... </two>? <one>Function</one>.
+- Ist die <one>Alpha-Helix</one> <two>rechts- oder linksgängig</two>? Die <one>Alpha-Helix</one> ist <two>rechtsgängig</two>.
+- Die <one>erste Röntgenstrukturanalyse bei einem Protein</one> überhaupt, erfolgte <two>an welchem Protein genau</two>? An <one>Myoglobin</one>. URL: https://de.wikipedia.org/wiki/Myoglobin
+- Does the human protein <one>transferrin</one> <two>tightly bind ferric iron</two>? <one>Yes</one> - this also <two>helps limit microbial growth</two>.
+- What is <one>the native structure of intrinsically disordered proteins</one> in general? They <one>do not adopt a (unique) native structure</one>.
+- Das erste Protein, dessen <one>atomare Struktur</one> <two>aufgeklärt werden konnte</two>, war ... ? A: <one>Myoglobin</one>. URL: https://de.wikipedia.org/wiki/Myoglobin
+- <two>Welche Formen</two> können <one>Beta-Faltblätter</one> einnehmen? A: <one>Parallel</one>, <one>antiparallel</one> und eine <one>Mischform</one> davon.
+- Give another term for <one>global prediction of all protein-protein interactions</one>. A: The <one>Interactome</one>. URL: https://en.wikipedia.org/wiki/Interactome
+- The basic repeating unit of a polypetide chain is ... ? <one>NH-Calpha-H-CO</one>.