PHAR 202 - Quaternary Structure

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16 Terms

1
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What is a quaternary structure

  • proteins that are composed for more than 1 polypeptide chain

2
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What is the molecular mass of proteins in quartenary structures

  • the spatial arrangements of these subunit arrangements

larger than 100kD

3
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Why is it useful for proteins to be made of multiple subunits instead of one large polypeptide?

Smaller subunits are easier to fold and manage.

4
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How do multi-subunit proteins deal with defective components?

A faulty subunit can be replaced without remaking the whole protein.

5
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What advantage does assembling proteins at different sites give?

Subunits can be synthesized in one place and assembled in another, giving flexibility.

6
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How is it more efficient to increase protein size through subunit association?

By reusing identical subunits instead of coding for one huge polypeptide.

7
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Where are the active sites often located in multimeric enzymes?

At the interfaces between subunits.

8
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How do multiple subunits help regulate protein activity?

They provide a structural basis for regulation

9
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What is a multimeric protein

a protein made of multiple individual protein subunits (polypeptide chain)

10
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<p>A multimeric protein may consist of identical or non-identical polypeptide chains, called</p>

A multimeric protein may consist of identical or non-identical polypeptide chains, called

homooligomers

heterooligomers

11
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How subunits stick together

when they associate, they bury 1000 to 2000 Ų, at least ~600 Ų surface area that would other wise be exposed to solvent

  • this results in them looking like the interior of a single subunit

12
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What are the similarities between two subunits sticking together and a single subunit?

  • closely packed non-polar side chains

  • hydrogen bonds

  • interchain disulfide bonds

13
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What are the differences between two subunits sticking together and a single subunit?

  • protein-protein interfaces

    • less hydrophobic bcs fewer hydrophobic patches

  • Hydrogen bonding patter

    • 77% happen between side chains (INTERSUBUNIT)

    • 68% happen between backbond (INTRASUBUNIT)

14
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Around …..% protein-protein interfaces contain salt bridge

56%

15
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Salt bridges contribute to the specificity and stability of

subunit associations

16
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Hydrophobic interactions and spaces offer ……… environments

Low dielectric constant