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proteins Flashcards

1
Q

unbranched polymer in which the monomer units are amino acids.

A

proteins

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2
Q

Is a peptide in which at least 40 amino acid residues are present.

A

proteins

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3
Q

these are messengers

A

hormones

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4
Q

it is the speed up reactions

A

enzymes

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5
Q

the “antinnae”

A

cell receptors

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6
Q

fight foreign invaders

A

antibodies

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7
Q

allowing specific molecules to enter or
leave a cell

A

MEMBRANE CHANNELS

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8
Q

is an amino acid in which the amino group

A

a-amino acid

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9
Q

CLASSIFICATION OF AMINO ACIDS ACCORDING TO SIDE CHAIN POLARITY

A

nonpolar amino acid, polar neutral amino acid, polar acidic amino acid, polar basic amino acid

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10
Q

an amino acid that contains one amino group, one carboxyl group, and a nonpolar side chain

A

nonpolar amino acid

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11
Q

an amino acid that contains one amino group, one carboxyl group, and a side chain that is polar but neutral

A

polar neutral amino acid

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12
Q

an amino acid that contains two amino groups and one carboxyl group, the second amino group being part of the side chain

A

polar basic amino acid

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13
Q

an amino acid that contains one amino group and two carboxyl groups, the second carboxyl group being part of the side chain

A

polar acidic amino acid

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14
Q

cysteine

A

Cys, C

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15
Q

histidine

A

His, H

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16
Q

isoleucine

A

Ile, I

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17
Q

methionine

A

Met, M

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18
Q

serine

A

Ser, S

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19
Q

valine

A

Val, V

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20
Q

alanine

A

Ala, A

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21
Q

glycine

A

Gly, G

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22
Q

leucine

A

Leu, L

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23
Q

proline

A

Pro, P

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24
Q

threonine

A

Thr, T

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25
Q

arginine

A

Arg ,R

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26
Q

asparagine

A

Asn, N

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27
Q

aspartate

A

Asp, D

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28
Q

glutamate

A

Glu, E

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29
Q

glutamine

A

Gln, Q

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30
Q

phenylalanine

A

Phe, F

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31
Q

tyrosine

A

Tyr, Y

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32
Q

tryptophan

33
Q

aspartate

34
Q

glutamate

35
Q

lysine

36
Q

hydrophobic side chain functional group

A

nonpolar amino acid

37
Q

uncharged, non-ionic side chains

A

polar neutral amino acid

38
Q

positively charged

A

polar basic amino acid

39
Q

negatively charged

A

polar acidic amino acid

40
Q

a standard amino acid needed for protein synthesis that must be obtained from dietary sources

A

ESSENTIAL AMINO ACIDS

41
Q

Synthesized by the body

A

NON-ESSENTIAL AMINO ACIDS

42
Q

occurs in people who have a severe protein deficiency

A

KWASHIORKOR

43
Q

children who developed this disorder are often older than children who develop marasmus

A

kwashiorkor

44
Q

symptoms of kwashiorkor

A

inability to grow or gain weight, edema, stomach bulging

45
Q

occurs more often in young children and babies. It leads to dehydration and weight loss

46
Q

starvation is a form of this disorder

47
Q

starvation is a form of this disorder

48
Q

symptoms of marasmus

A

weight loss, dehydration, stomach shrinkage

49
Q

found in the cell walls of many bacteria

A

D-glutamic acid

50
Q

found in earthworms

51
Q

one of the neurotransmitters in the brain

52
Q

a constituent of the vitamin pantothenic acid

A

β-alanine

53
Q

means double ion Is a molecule that has a positive charge on one atom

A

Zwitterion

54
Q

the pH at which an amino acid exists primarily in its zwitterion form.

A

ISOELECTRIC POINT

55
Q

a covalent bond (amide bond) between the carboxyl group of one amino acid

A

Peptide bond

56
Q

an unbranched chain of amino acids, each joined to the next by a peptide bond

57
Q

types of peptide

A

DOPT:
dipeptide
oligopeptide
polypeptide
tripeptide

58
Q

a compound containing two amino acids.

59
Q

three amino acids joined together in a chain.

A

Tripeptide

60
Q

refer to peptides with 10 to 20 amino acid residues.

A

Oligopeptide

61
Q

long unbranched chain of amino acids, each joined to the next by a peptide bond.

A

Polypeptide

62
Q

regulates uterine contraction and lactation, plays a role in stimulating the flow of milk in a nursing mother.

63
Q

regulates the excretion of water by the kidneys

A

Vasopressin

64
Q

pain killers (pentapeptide):neurotransmittersorneuromodulatorsatmanylocationsinthebrainandspinalcord

A

Enkephalins

65
Q

regulator of oxidation-reduction reaction

A

Glutathione

66
Q

the strongest bond

A

Peptide bond

67
Q

is a covalent bond between two sulfur.

A

Disulfide bond

68
Q

result from the attraction of electronegative atoms in the protein molecule.

A

Hydrogen Bond

69
Q

formed between groups which are positively and negatively charge.

A

Ionic bond

70
Q

formed by amino acids like leucine, valine, phenylalanine

A

Hydrophobic bond

71
Q

is a protein in which only one peptide chain is present.

A

monomeric protein

72
Q

is a protein in which more than one peptide chain is present.

A

multimeric protein

73
Q

a protein secondary structure in which a single protein chain adopts a shape

A

ALPHA HELIX

74
Q

Protein whose molecules have an elongated shape

75
Q

Protein whose molecules have peptide chains that are folded into spherical or globular shapes.

76
Q

is a protein that is found associated with a membrane system of a cell.

A

MEMBRANEOUS

77
Q

carries oxygen from the lungs to other organs and tissues

A

hemoglobin

78
Q

carries iron from the liver to the bone marrow

A

transferrin

biochem lec (5 decks)

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