Frage 1
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Define Protein Folding
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The process by which a protein obtains its natural 3D state
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The process by which a polypeptide chain is created from mRNA
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The process by which DNA sequences are converted into an mRNA chain
Frage 2
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Which structure of a protein shows biological activity?
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Primary
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Secondary
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Tertiary
Frage 3
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Which of the following occurs to ALL proteins?
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Non-covalent folding
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Covalent folding
Frage 4
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Which of the following are covalent modifications of the polypeptide chain?
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Glycosylation
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Phosphorylation
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Formation of disulphide bonds
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Van Der Waals interactions
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Electrostatic interactions
Frage 5
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Folding corresponds to a hierarchy of protein structure
Frage 6
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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
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A-B-C-G-D-H-F-E
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A-B-E-F-G-D-C-H
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A-D-C-B-E-F-H
Frage 7
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What is meant by the 'Thermodynamic Hypothesis of Protein Folding'
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That proteins fold into different structures based on the energy available to them in the medium
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That the information for correct protein folding is found within the sequence itself
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That the protein will always fold into the lowest possible energy state
Frage 8
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The Kinetic Hypothysis suggests that there is a specific folding pathway for each protein- protein folding is not random
Frage 9
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Describe the features of the RNAase Refolding experiment?
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RNAase is denatured with urea
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RNAase is denatured with detergent
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And an oxidising agent to remove the disulphide bridges
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And a reducing agent to remove the disulphide bridges
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Once the denaturing agents were removed and it was re-oxdised
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Once the denaturing agents were removed and it was re-reduced
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Protein fully reformed itself and worked
Frage 10
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How do we know the RNAase really was denatured during the experiment?
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If the protein was allowed to reform before the reducing agents were removed, the sequence showed non native sulphides and didn't work
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We don't know- we can never really KNOW anything
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If the protein was allowed to reform before the reducing agents were removed, the sequence didn't work
Frage 11
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Which of the following are conditions for In Vitro Refolding (Like in the RNAase experiment)?
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Structure must be amenable to environmental changes
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Free energy path must be relatively smooth
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Must contain covalent bonds
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Must have slow transitions
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Structure must have unique free energy
Frage 12
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What type of amino acid is being shown ere?
Frage 13
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Trans formations are less stable due to their steric hindrance
Frage 14
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Proline is added to an amino acid chain exclusively in what form?
Frage 15
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Which of the following proteins converts cis isomers to their trans form?
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Peptidyl Propyl Isomerases
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Peptidyl Glucyl Isomerases
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Peptidyl Lipyl Isomerases
Frage 16
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In the Cis form, the clash of functional groups around the alpha carbon is much greater due to steric hindrance
Frage 17
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What type of bond is being shown here?
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Disulphide
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Van Der Waals
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Electrostatic Attraction
Frage 18
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The previous amino acid to proline experiences steric hindrance in either proline conformation
Frage 19
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Cis proline has _ energy than/to trans proline
Frage 20
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The two cystine molecules that bind together are known as what?
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Cysteine
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Bi-cystine
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Bi-sulphur cystine
Frage 21
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Proteins with di-sulphide bonds are most likely to be found where?
Frage 22
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Phosphorylation occurs on which residues?
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Serine
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Valine
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Threonine
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Tyrosine
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Glutamine
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Asparagine
Frage 23
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Pro-sequences are found at the C-terminus
Frage 24
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The Pro-sequence is also known as
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A chaperone sequence
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A ligation sequence
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A glycosylation sequence
Frage 25
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Which proteins will have a pro-sequence?
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Chaperones
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Proteases
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Ligand-binding proteins
Frage 26
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The protein with a pro-sequence will auto-cleave it before folding correctly
Frage 27
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What is co-operativity in protein folding?
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Where one area of the protein that has already folded provides a nucleation site for another domain to fold
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The pre-formed proteins will be used as a template to fold more of that species
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Where chaperone proteins assist in protein folding
Frage 28
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What does the Hydrophobic Zipper Model suggest?
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That hydrophobic amino acids in close proximity are more likely to interact
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That hydrophillic amino acids in close proximity are more likely to interact
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Constraining the chain and making other residues more likely to interact, which further constrains the chain, etc.