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Biochemistry > Amino Acids and Proteins > Flashcards

Amino Acids and Proteins Flashcards

1
Q

building blocks of proteins

A

amino acids

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2
Q

general structure of amino acid

A

amino group
carboxylic acid
central alpha carbon

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3
Q

in this form the amino group is in the form of -NH2 and the carboxylic acid is in COOH

A

non-ionized form

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4
Q

form wherein the acid and basic functional groups are ionized (as -COO- and NH3+)

A

zwitterionic form

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5
Q

from where Net charge is still zero

A

zwitterionic form

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6
Q

draw a non-ionized form of an amino acid

A

grade yourself accordingly

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7
Q

draw a zwitterionic form of an amino acid

A

grade yourself accordingly

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8
Q

also known as side chain, which determines the identity and properties of an amino acids

A

R group

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9
Q

have neutral hydrophobic side chain and include the aliphatic amino acids, located inside the amino acid

A

non-polar amino acid

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10
Q

only nonchiral amino acid

A

glycine

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11
Q

secondary, cylic, imino acid

A

proline

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12
Q

aromatic amino acids

A

phenylalanine, tryptophan

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13
Q

sulfur-containing amino acid

A

cysteine
methionine

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14
Q

have neutral hydrophilic side chain particularly the amino acids, located outside the protein:

A

polar amino acid

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15
Q

neutral hydrophilic polar amino acid

A

serine
threonine

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16
Q

phenolic amino acid

A

tyrosine

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17
Q

amide amino acids

A

asparagine
glutamine

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18
Q

have polar and basic amino acid side chain which forms a positively charged ammonium group

A

positively charged amino acid

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19
Q

example of postively charged amino acid

A

lysine
arginine
histidine

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20
Q

have polar and acidic carboxylic acid side chain which forms a negatively-charged carboxylate group

A

aspartic acid
glutamic acid

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21
Q

Glycine 3 letter, 1 letter

A

Gly, G

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22
Q

Alanine 3 letter, 1 letter

A

Ala, A

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23
Q

Valine 3 letter 1 letter

A

Val, V

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24
Q

Leucine 3 letter 1 letter

A

Leu, L

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25
Q

Isoleucine 3 letter 1 letter

A

Ile, I

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26
Q

Cysteine 3 letter 1 letter

A

CYS, C

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27
Q

Proline 3 letter 1 letter

A

Pro, P

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28
Q

Tryptophan 3 letter 1 letter

A

Trp, W

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29
Q

Phenylalanine 3 letter 1 letter

A

Phe, F

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30
Q

Serine 3 letter 1 letter

A

Ser, S

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31
Q

Threonine 3 letter 1 letter

A

Thr, T

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32
Q

Tyrosine 3 letter 1 letter

A

Tyr, Y

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33
Q

Asparagine 3 letter 1 letter

A

Asn, N

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34
Q

Glutamine 3 letter 1 letter

A

Gln, Q

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35
Q

Aspartic acid

A

Asp, D

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36
Q

Glutamic Acid

A

Glu, E

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37
Q

Lysine

A

Lys, K

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38
Q

Arginine

A

Arg, R

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39
Q

Histidine

A

His, H

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40
Q

draw cysteine

A

grade yourself accordingly

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41
Q

draw glycine

A

grade yourself accordingly

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42
Q

draw alanine

A

grade yourself accordingly

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43
Q

draw valine

A

grade yourself accordingly

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44
Q

draw leucine

A

grade yourself accordingly

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45
Q

draw isoleucine

A

grade yourself accordingly

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46
Q

draw proline

A

grade yourself accordingly

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47
Q

draw methionine

A

grade yourself accordingly

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48
Q

draw tryptophan

A

grade yourself accordingly

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49
Q

draw phenylalanine

A

grade yourself accordingly

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50
Q

draw serine

A

grade yourself accordingly

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51
Q

draw threonine

A

grade yourself accordingly

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52
Q

draw tyrosine

A

grade yourself accordingly

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53
Q

draw asparagine

A

grade yourself accordingly

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54
Q

draw glutamine

A

grade yourself accordingly

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55
Q

draw aspartic acid

A

grade yourself accordingly

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56
Q

draw glutamic acid

A

grade yourself accordingly

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57
Q

draw lysine

A

grade yourself accordingly

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58
Q

draw arginine

A

grade yourself accordingly

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59
Q

draw histidine

A

grade yourself accordingly

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60
Q

nonpolar amino acid interaction with water

A

hydrophobic

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61
Q

amino acid that Contain O and S atoms, but no charge

A

polar, neutral

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62
Q

Contain carboxylate groups, negative charged

A

polar, acidic

63
Q

contain ammonium groups, positive charge

A

polar, basic

64
Q

Amino acids are also classified based on their nutritional requirements

A

essential
conditionally essential
nonessential amino acid

65
Q

those that are not synthesized by the body and therefore must be obtained from diet

A

essential amino acids

66
Q

essential amino acids

A

Histidine
Isoleucine
Leucine
Lysine
Methionine
Phenylalanine
Threonine
Tryptophan
Valine

67
Q

considered essential under certain circumstances of conditions, synthesis limited in case of stress/starvation/disease

A

conditionally essential

68
Q

example of conditionally essential

A

tyrosine
phenylalanine

69
Q

can be made in the body, not needed in diet

A

nonessential amino acids

70
Q

example of non-essential amino acids

A

Alanine
Asparagine
Aspartic acid
Glutamic acid
Arginine
Cysteine
Glutamine
Glycine
Proline
Serine
tyrosine

71
Q

proteins with significant amounts of all essential amino acids

A

complete proteins

72
Q

link amino acids with each other to form peptides and eventually protein

A

peptide bonds

73
Q

condenses with another amino group of another amino acid

A

carboxyl group

74
Q

peptide bond is also called this

A

amide bond

75
Q

side product of amine bond

A

h2o

76
Q

leftmost amino acid that has the free amino group

A

n-terminal end or terminus

77
Q

rightmost amino acid with the free carboxyl group

A

c-terminal end or terminus

78
Q

process where water molecule is released

A

dehydration/condensation

79
Q

peptide bond has a ___ bond that joins 2 amino acids

A

covalent bond

80
Q

release of H2O

A

dehydration

81
Q

peptide bond has a ___ double bond character: as shorter than a single bond

A

partial

82
Q

rotation around the bond is restricted because of this orientation

A

rigid and planar

83
Q

configuration of peptide bond where there is less steric hindrances of adjacent amino acid side chains

A

trans configuration

84
Q

peptide bond is charged what

A

uncharged

85
Q

Polar H atom of N-H amino group has partial ____ charge and polar O atom of C=O carboxyl group has partial ____charge

A

positive
negative

86
Q

Four reaction of amino acids

A

Reaction due to the amino group (-NH2)
Reaction due to carboxy group (-COOH)
Reaction due to both amino and carboxyl group
Reaction due to side chain

87
Q

catalyzed by an oxidase or dehydrogenase enzyme where amine is removed and a-keto acid is formed

A

oxidative deamination

88
Q

what is formed when amine is removed in oxidative deamination

A

a-keto acid

89
Q

Keto acid can be converted to what

A

glucose or ketone bodies

90
Q

transfer of an amino group to an a-keto to form another amino acid

A

transamination

91
Q

reaction takes place at alkaline pH and responsible for transfer of CO2 from the tissue to the lungs by hemoglobin

A

formation of carbamino compound

92
Q

removes CO2 in amino acids to produces amines

A

decarboxylation

93
Q

Amine formed in the decarboxylation process have ____ physiological activity

A

high

94
Q

reaction happens in the presence of NH3 where the a-carboxyl group of an amino acid will react to form the amide

A

formation of amide linkage

95
Q

happens in the presence of ammonia

A

formation of amide linkage

96
Q

phosphate groups react with amino acids containing the hydroxyl group, -OH, to form phosphoproteins

A

ester formation

97
Q

Happens in serine, threonine, tyrosine

A

ester formation

98
Q

when an amino acid attaches to a carbohydrate

A

glycoside formation

99
Q

reaction involves the amino acid cysteine when it forms disulfide linkages called disulfide bonds

A

reaction due to -SH group (disulfide bond formation)

100
Q

involves the transfer of the methyl group of methionine to produce other biological compounds

A

transmethylation

101
Q

formation of norepinephrine to epinephrine

A

transmethylation

102
Q

important neurotransmitter that is synthesized from phenylalanine or tyrosine using hydroxylase and decarboxylase enzymes

A

dopamine

103
Q

Binds to dopaminergic receptors and plays a role as a reward center of the brain

A

dopamine

104
Q

Function in memory, mood, motivation, and control of movement

A

dopamine

105
Q

deficiency in dopamine is associated with this, a progressive disorder that results to loss of muscular movement control

A

Parkinson’s disease

106
Q

Also associated with Hutington’s disease, schizophrenia, attention deficit/hyperactivity disorder (ADHD), and addiction

A

dopamine

107
Q

dopamine made in what areas of the brain

A

substantia nigra
hypothalamus
ventral tegmental area

108
Q

chemical messengers that your body can’t function without

A

neurotransmitter

109
Q

molecules where neurotransmitter binds. Relay signal carried from one cell to another

A

receptors

110
Q

dopamine from this is released when receiving an award

A

ventral tegmental area

111
Q

dopamine released associated with movements and speech

A

substantia nigra

112
Q

the ventral tegmental area projects dopamine to the nucleus accumbens

A

mesolimbic pathway

113
Q

dopamine moves from the ventral tegmental area to the prefrontal cortex

A

mesocortical pathway

114
Q

dopamine projects from substantia nigra to caudate putamen nucleus

A

nigrostriatal pathway

115
Q

sends dopamine from hypothalamus to pituitary gland

A

tuberoinfundibular pathway

116
Q

more popularly known as adrenaline, the fight or flight hormone that is synthesized in the adrenal gland

A

epinephrine

117
Q

Released during stressful conditions or emergencies, creates the “adrenaline rush

A

epinephrine

118
Q

characterized by heartbeat elevation, increase in blood flow to the muscles, and blood sugar elevation by release of glucose from glycogen reserves

A

adrenaline rush

119
Q

Used in medicine for treatment of severe allergy called anaphylaxis and cardiac arrest

A

epinephrine

120
Q

Also acts as an excitatory neurotransmitter in a small number of neurons

A

epinephrine

121
Q

pair of endocrine glands found atop the kidneys

A

adrenal gland

122
Q

immediate precursor of epinephrine and is also known as noradrenaline

A

norepinephrine

123
Q

Both hormonal and neurotransmitter function

A

norephinephrine

124
Q

it is responsible for fight-or-flight response as in andrenaline

A

norepinephrine

125
Q

As a neurotransmitter, it increases libido or sexual arousal, heightens alertness and vigilance, and hastens memory formation and retrieval

A

norepinephrine

126
Q

dopamine, epinephrine, and norepinephrine are called this as they are derived from cathecol

A

cathecolamines

127
Q

derived from amino acids phenylalanine or tyrosine

A

catechol

128
Q

label the compounds and eznymes

A

grade yourself accordingly

128
Q

important neurotransmitter that is synthesized from the amino acid tryptophan via hydroxylase and decarboxylase enzymes

A

serotonin

128
Q

Synthesized in the gastrointestinal tract (GI) by the enterochromaffin cells for regulation of intestinal movements

A

serotonin

129
Q

where 2 percent of serotonin was synthesized, playing a vital role in the regulation of mood, sleep, and appetite

A

central nervous system

130
Q

where serotonin neurons are found

A

raphe nuclei

131
Q

6 families of serotonin receptors are what

A

g-protein coupled receptors

132
Q

1 family of serotonin receptors consist of

A

ligan-gated ion channels

133
Q

naturally occurring tripeptide that has potent antioxidant property

A

glutathione

134
Q

Become a popular ingredient in various whitening pills and cosmetic products

A

glutathione

135
Q

glutathione amino acid

A

y-glutamylcysteinylglycine tripeptide

136
Q

Most abundant non-protein thiol in mammalian tissues with millimolar concentrations

A

glutathione

137
Q

Acts as a regulator of cellular redox state protecting cells from damage caused by lipid peroxides, reactive oxygen, and nitrogen species, and xenobiotics

A

glutathione

138
Q

Important in key signal transduction reactions as a controller of cell differentiation, proliferation, apoptosis, ferroptosis, and immune function

A

glutathione

139
Q

nonapeptide hormone and neuropeptide that is composed of Cys-Tyr-Ile-Gln-Asn-Cys-Pro-Leu-Gly-NH2

A

oxytocin

140
Q

nonapeptide of oxytocin

A

Cys-Tyr-Ile-Gln-Asn-Cys-Pro-Leu-Gly-NH2

141
Q

Produced in the hypothalamus and released by the posterior pituitary gland primarily during and after childbirth to stimulate uterine contractions and lactation

A

oxytocin

142
Q

Acts as a chemical messenger in the brain and affects human and mammalian behavior such as parent-infant bonding, feeling of trust, mood elevation, romantic attachment, and sexual arousal

A

oxytocin

143
Q

Available in injectable form for inducing child labor, and intranasal spray of psychiatric, hormonal, and even weight management

A

oxytocin

144
Q

Produced in the hypothalamus and transported through axons to the posterior lobe of pituitary gland

A

oxytocin

145
Q

ver of oxytocin may be involved with trust, empathy, and social bonding

A

centrally released oxytocin

146
Q

nonapeptide hormone and neuropeptide but is composed of Cys-Tyr-Phe-Gln-Asn-Cys-Pro-Arg-Gly-NH2 where phenylalanine and arginine are different amino acid from that of oxytocin

A

vasopressin

147
Q

nonapeptide of vasopression

A

Cys-Tyr-Phe-Gln-Asn-Cys-Pro-Arg-Gly-NH2

148
Q

is also produced in the hypothalamus and released by the posterior pituitary gland but it functions as an antidiuretic hormone (ADH)

A

vasopressin

149
Q

vasopressin is also known as

A

arginine vasopressin (AVO)

150
Q

As an ADH it stimulates the kidney tubules to increase water reabsorption and thus decreases the urine volume. It also raises arterial blood pressure and peripheral vascular resistance, resulting to an increase in the blood pressure (hypertension).

A

vasopressin

151
Q

Similar to oxytocin, it also acts as neuropeptides and affect complex human and mammalian social behaviors such as pair bonding, social recognition and aggression causally increases humans’ willingness to engage in risky, mutually beneficial cooperation

A

vasopressin

152
Q
A

Biochemistry (12 decks)

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