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Flashcards in Protein Faltung Deck (16)
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1
Q

Was sind 1. 2. 3. 4. Protein Faltungen?

A

?

2
Q

Proteins are synthesised at ribosomes with a rate of 20 AA / s

A

-

3
Q

Partial double-bond character of peptide (C-N) bond keeps that in a plane with carbonyl.

A

Cα-N-bond (Φ) and the Cα-C bond (Ψ)

4
Q

Anfinsen’s Dogma – folding code

Each protein has only one structure, with the lowest energy, determined by its primary sequence.

A

-

5
Q

Levinthal’s Paradox –folding speed

A

Calculation

6
Q

Faltung

A

= freie Drehbarkeit der Einfachbindungen der Haupt- und Seitenketten (Rotationsprozess)

7
Q

Bond strength

A

NOTES

8
Q

most common interactions in folded proteins (Hydrophobic interaction, Hydrogen bonds and Electrostatic interaction) are all favoured by the exclusion of water!

A

-

9
Q

?The Molten Globule State?

A

Notes?

10
Q

Compactness promotes native folding

A

proteins with a ratio of H:P of 1:1 fold rather well

11
Q

Folding routes as determined by the zipping and assembly method (ZAM). Small pieces that fold fast come together.

A

Entropy is dominant in larger proteins ➜ release of more free water

12
Q

Calculation and approximation of an energy surface

A

The folding process is reflected by a progress variable Q, defined as the fraction of native state contacts that are present at a given state of folding. Q is plotted vs. Energy E and available space P (pressure). (EQP-diagram).

13
Q

Levinthal-Paradox – Faltungsgeschwindigkeit:

A

= beschreibt die zunehmende Komplexität der Proteinfaltung zum Erreichen einer bestimmten Proteinstruktur bei zunehmender Kettenlänge

14
Q

Chaperone

A

Chaperone sind Proteine, die anderen Proteinen helfen ihre endgültige aktive Konformation zu finden (korrektes Erscheinungsbild), ohne Teil des Endzustandes zu sein (z.B. Hitzeschockproteine; HPS70, HSP90 etc.) = „Faltungshelfer“

15
Q

What does Levinthal’s paradox say? Is folding in series or in parallel?

A

VL script 12

16
Q

Other questions on VL 12 Script

A

undone ?