proteins Flashcards

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1
Q

backbone of polypeptide chain is

A

atoms that make up the covalent linkages from amino acid to next - everything but R groups

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2
Q

bonds that exist in primary protein structure

A

cov between backbone atoms

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3
Q

secondary structure of proteins

A

alpha helix and beta pleated sheet from nc interactions with nearby amino acids

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4
Q

all bonds present in secondary protein structure

A

covalent between backbone, nc between backbone

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5
Q

all bonds present in secondary protein structure

A

covalent between backbone, nc between backbone

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6
Q

tertiary protein structure

A

3D shape of a polypeptide

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7
Q

bonds present in tertiary protein structure

A

covalent between backbone, nc between backbone, covalent between R groups, nc between backbone and r groups, nc between r groups

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8
Q

quaternary protein structure

A

structure formed by interactions between multiply polypeptides via nc interactions

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9
Q

integral membrane proteins

A

transmembrane proteins span entire membrane

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10
Q

peripheral membrane proteins

A

associated w lipid bilayer on either side, anchored by anchor proteins

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11
Q

protein denaturation

A

loss of biological activity from protein unfolding, disruptions of non covalent interactions

change in pH, temp etc

proteins w/ strong interactions between side chains more difficult to denature

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12
Q

protein renaturation

A

regaining activity

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13
Q

factors that may affect interactions between r groups

A

size of chain, number of interactions (many ID-ID could be strong), location of the protein (interior/exterior, water or no)

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14
Q

factors that may affect interactions between r groups

A

size of chain, number of interactions (many ID-ID could be strong), location of the protein (interior/exterior, water or no)

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15
Q

conformational changes

A

shape of protein changes when a small molecule binds to the active site OR another site, allosteric site

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16
Q

two types of allosteric changes

A

allosteric inhibition - substrate cannot bind because of conformational change caused by binding of inhibitor

allosteric activation - substrate CAN bind because of conformational change caused by binding of inhibitor