Chapter 4 Flashcards

1
Q

peptide bonds in proteins

A

trans

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2
Q

rotation in peptide chain

A

two covalent bonds of Ca-C (psi) and N-Ca(phi)

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3
Q

globular shapes

A

polypeptide chain must frequently reverse direction

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4
Q

globular proteins

A

compact, spherical, and conduct most enzymatic activity

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5
Q

fibrous proteins

A

extended, insoluble, and usually fill structural roles in the cell

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6
Q

intrinsically disordered protein

A

lack defined secondary and tertiary structure until bound

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7
Q

quaternary structure

A

assembly of individual polypeptides into a larger functional cluster

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8
Q

denaturation

A

loss of structural integrity with accompanying loss of activity

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9
Q

proteins can be denatured by

A

-heat or cold
-pH extremes
-organic solvents
-chaotropic agents

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10
Q

anfinsen ribonuclease refolding experiment

A

-urea in the presence of 2-mercaptoethanol fully denatures ribonuclease
- when they are removed, protein refolds and current disulfide bonds are reformed
- protein sequence alone determines the native conformation

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11
Q

chaperones

A

do not actively promote the folding of the substrate protein but prevent aggregation of unfolded peptides

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