Amino Acids, Peptides, Proteins Flashcards

1
Q

amino acids

A

four groups attached to a central (α) carbon; an amino group, a carboxylic acid group, a hydrogen atom, and an R group 20 appear in the proteins of eukaryotic organisms stereochemistry is L in eukaryotes, D can exist in prokaryotes hydrophobic - w/ long alkyl chains hydrophilic - w/ charges

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2
Q

R group

A

determines chemistry and function of that amino acid

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3
Q

cysteine

A

polar side chain only amino acid with (R) configuration

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4
Q

glycine

A

non-polar, non-aromatic side chain only amino acid that is not chiral has a H atom as its R group

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5
Q

non-polar, non-aromatic amino acids

A

glycine, alanine, valine, leucine, isoleucine, methionine, proline

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6
Q

aromatic

A

tryptophan, phenylalanine, tyrosine

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7
Q

polar

A

serine, threonine, asparagine, glutamine, cysteine

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8
Q

negatively charged (acidic)

A

aspartate, glutamate

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9
Q

positively charged (basic)

A

lysine, arginine, histidine

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10
Q

amphoteric

A

can accept or donate protons amino acids

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11
Q

pKa

A

pH at which half of the species is deprotonated [HA] = [A-]

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12
Q

zwitterion

A

neutral amino acid that exists at pH near the pI of the amino acid

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13
Q

isoelectric point (pI)

A

calculated by averaging the two pKa values of amino acid without a charged side chain

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14
Q

formation/breaking of peptide bond

A

condensation/hydration reaction–one molecule of water released 1. nucleophilic amino group of one amino acid attacks the electrophilic carbonyl group of another amino acid 2. amide bonds are rigid due to resonance hydrolysis reaction–one molecule of water added

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15
Q

primary structure

A

linear sequence of amino acids in a peptide and is stabilized by peptide bonds

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16
Q

secondary structure

A

local structure of neighboring amino acids, and is stabilized by hydrogen bonding between amino groups and nonadjacent carboxyl groups α-helices, ß-pleated sheets

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17
Q

α-helices

A

secondary structure of protein clockwise coils around a central axis

18
Q

ß-pleated sheets

A

secondary structure of protein rippled strands that can be parallel or antiparallel

19
Q

proline

A

non-polar, non-aromatic side chain can interrupt secondary structure because of its rigid cyclic structure

20
Q

tertiary structure

A

three-dimensional shape of a single polypeptide chain, and is stabilized by hydrophobic interactions, acid-base interactions (salt bridges), hydrogen bonding, and disulfide bonds

21
Q

hydrophobic interactions

A

tertiary structure of protein push hydrophobic R groups to the interior of a protein which increases entropy of the surrounding water molecules and creates a negative Gibbs free energy

22
Q

disulfide bonds

A

occur when two cysteine molecules are oxidized and create a covalent bond to form cystine

23
Q

quaternary structure

A

interaction between peptides in proteins that contain multiple subunits

24
Q

prosthetic group

A

attached molecule of a conjugated protein may be a metal ion, vitamin, lipid, carbohydrate, or nucleic acid

25
Q

denaturation

A

both heat and increasing solute concentration can lead to loss of three-dimensional protein structure

26
Q

alanine

A

non-polar, non-aromatic side chain

27
Q

valine

A

non-polar, non-aromatic side chain

28
Q

leucine

A

non-polar, non-aromatic side chain

29
Q

isoleucine

A

non-polar, non-aromatic side chain

30
Q

methionine

A

non-polar, non-aromatic side chain

31
Q

tryptophan

A

aromatic side chain

32
Q

phenylalanine

A

aromatic side chain

33
Q

tyrosine

A

aromatic side chain

34
Q

serine

A

polar side chain

35
Q

threonine

A

polar side chain

36
Q

asparagine

A

polar side chain

37
Q

glutamine

A

polar side chain

38
Q

aspartic acid (aspartate)

A

negatively charged side chain (acidic)

39
Q

glutamic acid (glutamate)

A

negatively charged side chain (acidic)

40
Q

arginine

A

positively charged side chain (basic)

41
Q

lysine

A

positively charged side chain (basic)

42
Q

histidine

A

positively charged side chain (basic)