proteins Flashcards

(78 cards)

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
arginine
Arg ,R
26
asparagine
Asn, N
27
aspartate
Asp, D
28
glutamate
Glu, E
29
glutamine
Gln, Q
30
phenylalanine
Phe, F
31
tyrosine
Tyr, Y
32
tryptophan
Trp, W
33
aspartate
Asx, B
34
glutamate
Glx, Z
35
lysine
Lys, K
36
hydrophobic side chain functional group
nonpolar amino acid
37
uncharged, non-ionic side chains
polar neutral amino acid
38
positively charged
polar basic amino acid
39
negatively charged
polar acidic amino acid
40
a standard amino acid needed for protein synthesis that must be obtained from dietary sources
ESSENTIAL AMINO ACIDS
41
Synthesized by the body
NON-ESSENTIAL AMINO ACIDS
42
occurs in people who have a severe protein deficiency
KWASHIORKOR
43
children who developed this disorder are often older than children who develop marasmus
kwashiorkor
44
symptoms of kwashiorkor
inability to grow or gain weight, edema, stomach bulging
45
occurs more often in young children and babies. It leads to dehydration and weight loss
marasmus
46
starvation is a form of this disorder
marasmus
47
starvation is a form of this disorder
marasmus
48
symptoms of marasmus
weight loss, dehydration, stomach shrinkage
49
found in the cell walls of many bacteria
D-glutamic acid
50
found in earthworms
D-serine
51
one of the neurotransmitters in the brain
GABA
52
a constituent of the vitamin pantothenic acid
β-alanine
53
means double ion Is a molecule that has a positive charge on one atom
Zwitterion
54
the pH at which an amino acid exists primarily in its zwitterion form.
ISOELECTRIC POINT
55
a covalent bond (amide bond) between the carboxyl group of one amino acid
Peptide bond
56
an unbranched chain of amino acids, each joined to the next by a peptide bond
Peptide
57
types of peptide
DOPT: dipeptide oligopeptide polypeptide tripeptide
58
a compound containing two amino acids.
dipeptide
59
three amino acids joined together in a chain.
Tripeptide
60
refer to peptides with 10 to 20 amino acid residues.
Oligopeptide
61
long unbranched chain of amino acids, each joined to the next by a peptide bond.
Polypeptide
62
regulates uterine contraction and lactation, plays a role in stimulating the flow of milk in a nursing mother.
Oxytocin
63
regulates the excretion of water by the kidneys
Vasopressin
64
pain killers (pentapeptide):neurotransmitters or neuromodulators at many locations in the brain and spinal cord 
Enkephalins
65
regulator of oxidation-reduction reaction
Glutathione
66
the strongest bond
Peptide bond
67
is a covalent bond between two sulfur.
Disulfide bond
68
result from the attraction of electronegative atoms in the protein molecule.
Hydrogen Bond
69
formed between groups which are positively and negatively charge.
Ionic bond
70
formed by amino acids like leucine, valine, phenylalanine
Hydrophobic bond
71
is a protein in which only one peptide chain is present.
monomeric protein
72
is a protein in which more than one peptide chain is present.
multimeric protein
73
a protein secondary structure in which a single protein chain adopts a shape
ALPHA HELIX
74
Protein whose molecules have an elongated shape
Fibrous
75
Protein whose molecules have peptide chains that are folded into spherical or globular shapes.
Globular
76
is a protein that is found associated with a membrane system of a cell.
MEMBRANEOUS
77
carries oxygen from the lungs to other organs and tissues
hemoglobin
78
carries iron from the liver to the bone marrow
transferrin