Supersecondary Structures & Energy Changes

Descripción

(Protein Folding) Structural Basis for Biological Function Test sobre Supersecondary Structures & Energy Changes, creado por gina_evans0312 el 19/12/2013.
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Test por gina_evans0312, actualizado hace más de 1 año
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Creado por gina_evans0312 hace casi 11 años
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Resumen del Recurso

Pregunta 1

Pregunta
Alpha helices are a helix-helix structure
Respuesta
  • True
  • False

Pregunta 2

Pregunta
Which of the following best describes an alpha helix?
Respuesta
  • Ridges are formed by side chains with troughs in between
  • Ridges are formed by the peptide bonds and the amino acid side chains form the troughs

Pregunta 3

Pregunta
Helix-helix packing can be shown by highlighting every _ residues?
Respuesta
  • 1st
  • 4th
  • 3rd
  • 2nd

Pregunta 4

Pregunta
Alpha helices must follow particular rules when packing together
Respuesta
  • True
  • False

Pregunta 5

Pregunta
Describe the ridges of the following proteins
Respuesta
  • i + 4
  • i + 2
  • i + 3

Pregunta 6

Pregunta
The angle between two packed helices depends on which type of ridges pack into which troughs.
Respuesta
  • True
  • False

Pregunta 7

Pregunta
The troughs of one alpha helix will be filled by the 'backbone' of another
Respuesta
  • True
  • False

Pregunta 8

Pregunta
Beta sheets twist slightly _ each other
Respuesta
  • Away from
  • Towards

Pregunta 9

Pregunta
The angle between two beta sheets is approx....?
Respuesta
  • 30 degrees
  • 60 degrees
  • 90 degrees

Pregunta 10

Pregunta
Where in the plane is each color (ignore green)
Respuesta
  • Yellow- above plane White- below plane
  • White- above plane Yellow- below plane
  • The amino acids will point in opposite directions

Pregunta 11

Pregunta
The strands of beta sheets are held together by backbone hydrogen bonding
Respuesta
  • True
  • False

Pregunta 12

Pregunta
The angle between sheets is determined by their...
Respuesta
  • Right handed twist
  • Left handed twist
  • Length
  • Amino acid side chains

Pregunta 13

Pregunta
How are the aa side chains arranged in beta sheets?
Respuesta
  • The amino acid residue side chains of one beta sheet pack between the spaces between side chains on the adjacent beta sheet
  • The amino acids on one beta sheet will have no residue where the other beta sheet has one (they're removed)
  • The amino acids with residues attached will alternate between beta sheets

Pregunta 14

Pregunta
When an alpha helix and a beta sheet pack together, the groove the beta sheet lies in tends to be made by amino acids how far apart?
Respuesta
  • 4n
  • 6n
  • 3n
  • 2n

Pregunta 15

Pregunta
Name three things that can be used in protein folding to encourage correct folding?
Respuesta
  • Non-native interactions (as long as they are reversible)
  • Pinching (isolates subdomains for folding)
  • The removal of a domain for folding, before it's re-addition

Pregunta 16

Pregunta
Negative Free Energy is less favorable
Respuesta
  • True
  • False

Pregunta 17

Pregunta
Concerning entropy- less order is more favorable
Respuesta
  • True
  • False

Pregunta 18

Pregunta
Which of the following is the equation for the free energy change of a folded protein
Respuesta
  • ΔG = ΔH - TΔS
  • ΔH = ΔG x TΔS
  • TΔS = ΔH + ΔG

Pregunta 19

Pregunta
Hydrogen bonds are the least common type of bond in proteins
Respuesta
  • True
  • False

Pregunta 20

Pregunta
What's the enthalpy change of a H bond formation?
Respuesta
  • -4 to -30 kJmol
  • -4 to -3 kJmol
  • -40 to -30 kJmol

Pregunta 21

Pregunta
A hydrophobic core in water is entropically favorable
Respuesta
  • True
  • False

Pregunta 22

Pregunta
Why is hydrophobic cores in water _favorable?
Respuesta
  • They make the water molecules more ordered, decreasing entropy
  • They make the water molecules less ordered, increasing entropy

Pregunta 23

Pregunta
Why do hydrophobic proteins fold?
Respuesta
  • Folded proteins have a reduced surface area, leading to a reduced number of organised water molecules, leading to a lower decrease of entropy
  • Folded proteins have a reduced surface area, leading to a reduced number of organised water molecules, leading to a lower increase of entropy

Pregunta 24

Pregunta
As water ordering decreases, entropy decreases
Respuesta
  • True
  • False

Pregunta 25

Pregunta
Why is energy needed to maintain the folding of a (hydrophobic) protein (i.e. from hydrogen bonds etc.)?
Respuesta
  • Because the unfolded state of the protein is more entropically favorable than the folded state
  • Because though the folded protein is more entropically favorable, it's folding decreases entropy, which is unfavorable
  • So energy must be produced to maintain the fold

Pregunta 26

Pregunta
Heating denatures a protein because it breaks the bonds required to offset the negative change in entropy caused by the protein folding i.e, it makes ΔH less negative
Respuesta
  • True
  • False

Pregunta 27

Pregunta
In protein folding, ΔH is negative, and -TΔS is positive
Respuesta
  • True
  • False
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