Protein Folding- The Basics

Beschreibung

Structural Basis for Biological Function (Protein Folding) Quiz am Protein Folding- The Basics, erstellt von gina_evans0312 am 19/12/2013.
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Quiz von gina_evans0312, aktualisiert more than 1 year ago
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Erstellt von gina_evans0312 vor etwa 11 Jahre
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Zusammenfassung der Ressource

Frage 1

Frage
Define Protein Folding
Antworten
  • 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

Frage 2

Frage
Which structure of a protein shows biological activity?
Antworten
  • Primary
  • Secondary
  • Tertiary

Frage 3

Frage
Which of the following occurs to ALL proteins?
Antworten
  • Non-covalent folding
  • Covalent folding

Frage 4

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

Frage 5

Frage
Folding corresponds to a hierarchy of protein structure
Antworten
  • True
  • False

Frage 6

Frage
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
Antworten
  • A-B-C-G-D-H-F-E
  • A-B-E-F-G-D-C-H
  • A-D-C-B-E-F-H

Frage 7

Frage
What is meant by the 'Thermodynamic Hypothesis of Protein Folding'
Antworten
  • 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

Frage 8

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

Frage 9

Frage
Describe the features of the RNAase Refolding experiment?
Antworten
  • 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

Frage 10

Frage
How do we know the RNAase really was denatured during the experiment?
Antworten
  • 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

Frage 11

Frage
Which of the following are conditions for In Vitro Refolding (Like in the RNAase experiment)?
Antworten
  • 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

Frage 12

Frage
What type of amino acid is being shown ere?
Antworten
  • Cis
  • Trans

Frage 13

Frage
Trans formations are less stable due to their steric hindrance
Antworten
  • True
  • False

Frage 14

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

Frage 15

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

Frage 16

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

Frage 17

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

Frage 18

Frage
The previous amino acid to proline experiences steric hindrance in either proline conformation
Antworten
  • True
  • False

Frage 19

Frage
Cis proline has _ energy than/to trans proline
Antworten
  • Greater
  • Less
  • Equal

Frage 20

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

Frage 21

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

Frage 22

Frage
Phosphorylation occurs on which residues?
Antworten
  • Serine
  • Valine
  • Threonine
  • Tyrosine
  • Glutamine
  • Asparagine

Frage 23

Frage
Pro-sequences are found at the C-terminus
Antworten
  • True
  • False

Frage 24

Frage
The Pro-sequence is also known as
Antworten
  • A chaperone sequence
  • A ligation sequence
  • A glycosylation sequence

Frage 25

Frage
Which proteins will have a pro-sequence?
Antworten
  • Chaperones
  • Proteases
  • Ligand-binding proteins

Frage 26

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

Frage 27

Frage
What is co-operativity in protein folding?
Antworten
  • 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

Frage 28

Frage
What does the Hydrophobic Zipper Model suggest?
Antworten
  • 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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