Protein Folding- The Basics

Descrição

Structural Basis for Biological Function (Protein Folding) Quiz sobre Protein Folding- The Basics, criado por gina_evans0312 em 19-12-2013.
gina_evans0312
Quiz por gina_evans0312, atualizado more than 1 year ago
gina_evans0312
Criado por gina_evans0312 aproximadamente 11 anos atrás
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Resumo de Recurso

Questão 1

Questão
Define Protein Folding
Responda
  • The process by which a protein obtains its natural 3D state
  • The process by which a polypeptide chain is created from mRNA
  • The process by which DNA sequences are converted into an mRNA chain

Questão 2

Questão
Which structure of a protein shows biological activity?
Responda
  • Primary
  • Secondary
  • Tertiary

Questão 3

Questão
Which of the following occurs to ALL proteins?
Responda
  • Non-covalent folding
  • Covalent folding

Questão 4

Questão
Which of the following are covalent modifications of the polypeptide chain?
Responda
  • Glycosylation
  • Phosphorylation
  • Formation of disulphide bonds
  • Van Der Waals interactions
  • Electrostatic interactions

Questão 5

Questão
Folding corresponds to a hierarchy of protein structure
Responda
  • True
  • False

Questão 6

Questão
Put the following in Order A -Unfolded B - Nucleation C - Secondary Structure D - Domain E - Active Oligomer F - Inactive Oligomer G - Supersecondary Structure H - Folded Monomer
Responda
  • A-B-C-G-D-H-F-E
  • A-B-E-F-G-D-C-H
  • A-D-C-B-E-F-H

Questão 7

Questão
What is meant by the 'Thermodynamic Hypothesis of Protein Folding'
Responda
  • That proteins fold into different structures based on the energy available to them in the medium
  • That the information for correct protein folding is found within the sequence itself
  • That the protein will always fold into the lowest possible energy state

Questão 8

Questão
The Kinetic Hypothysis suggests that there is a specific folding pathway for each protein- protein folding is not random
Responda
  • True
  • False

Questão 9

Questão
Describe the features of the RNAase Refolding experiment?
Responda
  • RNAase is denatured with urea
  • RNAase is denatured with detergent
  • And an oxidising agent to remove the disulphide bridges
  • And a reducing agent to remove the disulphide bridges
  • Once the denaturing agents were removed and it was re-oxdised
  • Once the denaturing agents were removed and it was re-reduced
  • Protein fully reformed itself and worked

Questão 10

Questão
How do we know the RNAase really was denatured during the experiment?
Responda
  • If the protein was allowed to reform before the reducing agents were removed, the sequence showed non native sulphides and didn't work
  • We don't know- we can never really KNOW anything
  • If the protein was allowed to reform before the reducing agents were removed, the sequence didn't work

Questão 11

Questão
Which of the following are conditions for In Vitro Refolding (Like in the RNAase experiment)?
Responda
  • Structure must be amenable to environmental changes
  • Free energy path must be relatively smooth
  • Must contain covalent bonds
  • Must have slow transitions
  • Structure must have unique free energy

Questão 12

Questão
What type of amino acid is being shown ere?
Responda
  • Cis
  • Trans

Questão 13

Questão
Trans formations are less stable due to their steric hindrance
Responda
  • True
  • False

Questão 14

Questão
Proline is added to an amino acid chain exclusively in what form?
Responda
  • Trans
  • Cis
  • The other form occurs 10-40% of the time, and must be altered post addition

Questão 15

Questão
Which of the following proteins converts cis isomers to their trans form?
Responda
  • Peptidyl Propyl Isomerases
  • Peptidyl Glucyl Isomerases
  • Peptidyl Lipyl Isomerases

Questão 16

Questão
In the Cis form, the clash of functional groups around the alpha carbon is much greater due to steric hindrance
Responda
  • True
  • False

Questão 17

Questão
What type of bond is being shown here?
Responda
  • Disulphide
  • Van Der Waals
  • Electrostatic Attraction

Questão 18

Questão
The previous amino acid to proline experiences steric hindrance in either proline conformation
Responda
  • True
  • False

Questão 19

Questão
Cis proline has _ energy than/to trans proline
Responda
  • Greater
  • Less
  • Equal

Questão 20

Questão
The two cystine molecules that bind together are known as what?
Responda
  • Cysteine
  • Bi-cystine
  • Bi-sulphur cystine

Questão 21

Questão
Proteins with di-sulphide bonds are most likely to be found where?
Responda
  • In low/high pH
  • Extracellular proteins
  • Cytoplasmic proteins
  • In low/high salt concentrations

Questão 22

Questão
Phosphorylation occurs on which residues?
Responda
  • Serine
  • Valine
  • Threonine
  • Tyrosine
  • Glutamine
  • Asparagine

Questão 23

Questão
Pro-sequences are found at the C-terminus
Responda
  • True
  • False

Questão 24

Questão
The Pro-sequence is also known as
Responda
  • A chaperone sequence
  • A ligation sequence
  • A glycosylation sequence

Questão 25

Questão
Which proteins will have a pro-sequence?
Responda
  • Chaperones
  • Proteases
  • Ligand-binding proteins

Questão 26

Questão
The protein with a pro-sequence will auto-cleave it before folding correctly
Responda
  • True
  • False

Questão 27

Questão
What is co-operativity in protein folding?
Responda
  • Where one area of the protein that has already folded provides a nucleation site for another domain to fold
  • The pre-formed proteins will be used as a template to fold more of that species
  • Where chaperone proteins assist in protein folding

Questão 28

Questão
What does the Hydrophobic Zipper Model suggest?
Responda
  • That hydrophobic amino acids in close proximity are more likely to interact
  • That hydrophillic amino acids in close proximity are more likely to interact
  • Constraining the chain and making other residues more likely to interact, which further constrains the chain, etc.

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