Protein Folding- The Basics

Descripción

(Protein Folding) Structural Basis for Biological Function Test sobre Protein Folding- The Basics, 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 alrededor de 11 años
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Resumen del Recurso

Pregunta 1

Pregunta
Define Protein Folding
Respuesta
  • 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

Pregunta 2

Pregunta
Which structure of a protein shows biological activity?
Respuesta
  • Primary
  • Secondary
  • Tertiary

Pregunta 3

Pregunta
Which of the following occurs to ALL proteins?
Respuesta
  • Non-covalent folding
  • Covalent folding

Pregunta 4

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

Pregunta 5

Pregunta
Folding corresponds to a hierarchy of protein structure
Respuesta
  • True
  • False

Pregunta 6

Pregunta
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
Respuesta
  • A-B-C-G-D-H-F-E
  • A-B-E-F-G-D-C-H
  • A-D-C-B-E-F-H

Pregunta 7

Pregunta
What is meant by the 'Thermodynamic Hypothesis of Protein Folding'
Respuesta
  • 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

Pregunta 8

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

Pregunta 9

Pregunta
Describe the features of the RNAase Refolding experiment?
Respuesta
  • 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

Pregunta 10

Pregunta
How do we know the RNAase really was denatured during the experiment?
Respuesta
  • 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

Pregunta 11

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

Pregunta 12

Pregunta
What type of amino acid is being shown ere?
Respuesta
  • Cis
  • Trans

Pregunta 13

Pregunta
Trans formations are less stable due to their steric hindrance
Respuesta
  • True
  • False

Pregunta 14

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

Pregunta 15

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

Pregunta 16

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

Pregunta 17

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

Pregunta 18

Pregunta
The previous amino acid to proline experiences steric hindrance in either proline conformation
Respuesta
  • True
  • False

Pregunta 19

Pregunta
Cis proline has _ energy than/to trans proline
Respuesta
  • Greater
  • Less
  • Equal

Pregunta 20

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

Pregunta 21

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

Pregunta 22

Pregunta
Phosphorylation occurs on which residues?
Respuesta
  • Serine
  • Valine
  • Threonine
  • Tyrosine
  • Glutamine
  • Asparagine

Pregunta 23

Pregunta
Pro-sequences are found at the C-terminus
Respuesta
  • True
  • False

Pregunta 24

Pregunta
The Pro-sequence is also known as
Respuesta
  • A chaperone sequence
  • A ligation sequence
  • A glycosylation sequence

Pregunta 25

Pregunta
Which proteins will have a pro-sequence?
Respuesta
  • Chaperones
  • Proteases
  • Ligand-binding proteins

Pregunta 26

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

Pregunta 27

Pregunta
What is co-operativity in protein folding?
Respuesta
  • 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

Pregunta 28

Pregunta
What does the Hydrophobic Zipper Model suggest?
Respuesta
  • 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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