Copy and Edit

Supersecondary Structures & Energy Changes

Description

Structural Basis for Biological Function (Protein Folding) Quiz on Supersecondary Structures & Energy Changes, created by gina_evans0312 on 19/12/2013.
gina_evans0312
Quiz by gina_evans0312, updated more than 1 year ago
gina_evans0312
Created by gina_evans0312 over 10 years ago
474
1
0

Resource summary

Question 1

Question
Alpha helices are a helix-helix structure
Answer
  • True
  • False

Question 2

Question
Which of the following best describes an alpha helix?
Answer
  • 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

Question 3

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

Question 4

Question
Alpha helices must follow particular rules when packing together
Answer
  • True
  • False

Question 5

Question
Describe the ridges of the following proteins
Image:
Ridges (image/png)
Answer
  • i + 4
  • i + 2
  • i + 3

Question 6

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

Question 7

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

Question 8

Question
Beta sheets twist slightly _ each other
Answer
  • Away from
  • Towards

Question 9

Question
The angle between two beta sheets is approx....?
Answer
  • 30 degrees
  • 60 degrees
  • 90 degrees

Question 10

Question
Where in the plane is each color (ignore green)
Image:
Beta_Sheet_Packing (image/png)
Answer
  • Yellow- above plane White- below plane
  • White- above plane Yellow- below plane
  • The amino acids will point in opposite directions

Question 11

Question
The strands of beta sheets are held together by backbone hydrogen bonding
Answer
  • True
  • False

Question 12

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

Question 13

Question
How are the aa side chains arranged in beta sheets?
Answer
  • 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

Question 14

Question
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?
Answer
  • 4n
  • 6n
  • 3n
  • 2n

Question 15

Question
Name three things that can be used in protein folding to encourage correct folding?
Answer
  • 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

Question 16

Question
Negative Free Energy is less favorable
Answer
  • True
  • False

Question 17

Question
Concerning entropy- less order is more favorable
Answer
  • True
  • False

Question 18

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

Question 19

Question
Hydrogen bonds are the least common type of bond in proteins
Answer
  • True
  • False

Question 20

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

Question 21

Question
A hydrophobic core in water is entropically favorable
Answer
  • True
  • False

Question 22

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

Question 23

Question
Why do hydrophobic proteins fold?
Answer
  • 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

Question 24

Question
As water ordering decreases, entropy decreases
Answer
  • True
  • False

Question 25

Question
Why is energy needed to maintain the folding of a (hydrophobic) protein (i.e. from hydrogen bonds etc.)?
Answer
  • 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

Question 26

Question
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
Answer
  • True
  • False

Question 27

Question
In protein folding, ΔH is negative, and -TΔS is positive
Answer
  • True
  • False
Show full summary Hide full summary

Want to create your own Quizzes for free with GoConqr? Learn more.

Similar

Protein Folding- The Basics
gina_evans0312
Constituative Chaperones
gina_evans0312
Chaperonins
gina_evans0312
Heat Shock Proteins
gina_evans0312
Molecular Chaperones in Bacteria, Yeast & Mammals
gina_evans0312
Glycosylation
gina_evans0312
Properties of Chaperones
gina_evans0312
Molecular Motors- Helicases
gina_evans0312
Protein Structure Pt. 1
gina_evans0312
Motor Proteins- Myosin
gina_evans0312
Motor Proteins- Kinesin
gina_evans0312
Browse Library