BSCI330: Protein Shape and Structure

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14 Terms

1
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What are the 4 levels of protein structure?

primary, secondary, tertiary, and quartnernary

<p>primary, secondary, tertiary, and quartnernary</p>
2
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What is the primary structure?

Linear sequence of amino acids!

Determine by mRNA code; in combination with environment can determine higher level structures

<p>Linear sequence of amino acids!</p><p>Determine by mRNA code; in combination with environment can determine higher level structures</p>
3
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Is the amino acid sequence of every protein identical to the genetically encoded primary sequence?

Yes!

4
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What is the secondary structure?

Folding and twisting of the peptide backbone

Held by H-bonds between carbonyl and amine groups

R-groups stick out from backbone

  • Alpha helices and beta sheets

<p>Folding and twisting of the peptide backbone</p><p>Held by H-bonds between carbonyl and amine groups</p><p>R-groups stick out from backbone</p><ul><li><p>Alpha helices and beta sheets</p></li></ul><p></p>
5
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What is the alpha helix?

H-bonding that occurs between carbonyl and amino groups that are 4 amino acids apart (spacing for the turn of a helix)!

Coiling in a clockwise direction!

<p>H-bonding that occurs between carbonyl and amino groups that are 4 amino acids apart (spacing for the turn of a helix)!</p><p>Coiling in a clockwise direction!</p>
6
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What is the beta sheet?

Pleated sheet like an accordion; H-bonding of carbonyl and amino groups on adjacent polypeptide chains

Can be parallel or anti-parallel!

<p>Pleated sheet like an accordion; H-bonding of carbonyl and amino groups on adjacent polypeptide chains</p><p>Can be parallel or anti-parallel!</p>
7
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Adjacent parallel v. anti-parallel chains (beta sheets)?

Parallel - Run N-terminal to C-terminal and must loop around

Anti-Parallel - Run N to C and in opposite directions (zig-zag terminals)

<p><strong>Parallel </strong>- Run N-terminal to C-terminal and must loop around </p><p><strong>Anti-Parallel </strong>- Run N to C and in opposite directions (zig-zag terminals)</p>
8
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What is the tertiary structure?

Mostly held down by noncovalent attractions between R-groups and surrounding environment.

Unstructured loops (aka random coils) like the secondary structures together!

<p>Mostly held down by noncovalent attractions between R-groups and surrounding environment.</p><p>Unstructured loops (aka random coils) like the secondary structures together!</p>
9
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What do covalent dissulfide bonds do?

They lock tertiary structures by forming between cysteine residues to cross-link parts of the polypeptide backbone.

<p>They lock tertiary structures by forming between cysteine residues to cross-link parts of the polypeptide backbone. </p>
10
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What determines 3D folding of proteins?

They will attempt to assume the lowest possible energy state! Protein stability is determined by the free energy change between folded and unfolded states!

<p>They will attempt to assume the lowest possible energy state! Protein stability is determined by the free energy change between folded and unfolded states!</p>
11
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What are molecular chaperones or chaperonins?

Provide an isolated chemical environment in which proteins can fold!

<p>Provide an isolated chemical environment in which proteins can fold!</p>
12
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What are protein domains?

A region of the protein that folds independently of other regions! Often represents a fucntional region of the protein!

<p>A region of the protein that folds independently of other regions! Often represents a fucntional region of the protein!</p>
13
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What are quaternary structures?

Arrangement of multiple tertiary stryuctures (weakly bonded, some with disulphide bonds)

14
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What are homomers and heteromers?

Identical (homomers) and different (heteromers) subunit polypeptides!

<p>Identical (homomers) and different (heteromers) subunit polypeptides!</p>

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