Protein and Amino Acid and Enzymes Flashcards

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1
Q

primary structure

A

amino acids– covalent bonds

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2
Q

secondary structure

A

hydrogen bond
alpha helices and beta pleated sheets

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3
Q

tertiary structure

A

ionic bonds, dipole-dipole, london dispersion and covalent interaction between amino acids

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4
Q

quaternary structure

A

disulfide bonds, london dispersion, dipole dipole,

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5
Q

what do kinase proteins do

A

they phosphorylate proteins

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6
Q

What properties exist for tyrosin

A

polar aromatic

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7
Q

which amino acid codes the start codon

A

methonine

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8
Q

how to determine the pI of a structure

A

Pka1+Pka2/2

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9
Q

what is a stereocenter

A

an atom that is bonded to 4 different subsitutents (chiral atom)

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10
Q

what is the only achiral amino acid

A

glycine (Gly, G) hydrophobic

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11
Q

what is average molecular weight of amino acid

A

110Da

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12
Q

what is a zymogen

A

active upon cleavage or modificaton

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13
Q

what does competitive inhibitor do to kinetics

A

increase Km, does not change V max

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14
Q

at low substrate addition of more substrate will

A

increase the rate linearly as it approaches vmax it will increase non linearly, but will not effect rate or vmax when reached

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15
Q

how are cyestine disulfide bridge formed or broken

A

REDOX

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16
Q

What is the termination process in protein synthesis

A

STOP codon–> release factors officially end protein synthesis

17
Q

what does noncompetitive inhibitors do to enzyme kinetics

A

do not change the Km though they do decrease the Vmax

18
Q

how do you calculate pI?

A

the average of the Pka values

19
Q

how to identify a stereocenter

A

attached to 4 unique molecular groups

20
Q

what is an achiral amino acid

A

glycine

21
Q
A