Proteins Flashcards

1
Q

Proteins

A

20 amino acids

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2
Q

non polar

A

hydrophobic and with two hydrocarbon side chains

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3
Q

polar

A

hydrophilic with ionic side chains

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4
Q

peptide bond

A

links two ore more amino acids together

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5
Q

amino acid

A

n-c-c

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6
Q

Primary Structure

A

sequence of amino acids

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7
Q

Secondary Structure

A

Alpha Helix, Beta Plate Sheet

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8
Q

Tertiary Structure

A

Globular proteins

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9
Q

Quanternary Structure

A

two globular proteins held together

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10
Q

Denaturation

A

the disruption of bonds in secondary, tertiary and quantary structures

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11
Q

Enyzmes

A

Biological Catalysts

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12
Q

oxidreduces

A

oxidation/reduction

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13
Q

Transferases

A

transfer of atoms

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14
Q

Lyases

A

ass/remove from a double bond

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15
Q

Hydrolases

A

Hydrolysis

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16
Q

Isomerases

A

rearrange atoms

17
Q

Ligases

A

use ATP to combine small molecules

18
Q

active site

A

where the substrate catalyzes the reaction

19
Q

lock and key model

A

active site is rigid, non flexible shape only for the substrate to fit in

20
Q

Induced fit model

A

enzy,e changes shape to fit the substrate more tightly

21
Q

optimum Ph for enzymes

A

7.4

22
Q

optimum temp for enzymes

A

37 C

23
Q

Competitive inhibitors

A

inhibitor fights the substrate and forms in the active site

24
Q

non competitive inhibitor

A

goes to the other side of a enzyme to change its shape of the active site

25
Q

hydrophobic interactions

A

two non polar amino acids

26
Q

hydrophilic interactions

A

between the external aqueous environment and R groups of polar amino acids

27
Q

Salt Bridges

A

between ionized R groups of basic and acidic amino acids

28
Q

Hydrogen Bonds

A

between H of a polar group

29
Q

disulfide bonds

A

between SH group and cysteine amino acids