Amino Acids and Proteins Flashcards
(154 cards)
1
Q
building blocks of proteins
A
amino acids
2
Q
general structure of amino acid
A
amino group
carboxylic acid
central alpha carbon
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
4
Q
form wherein the acid and basic functional groups are ionized (as -COO- and NH3+)
A
zwitterionic form
5
Q
from where Net charge is still zero
A
zwitterionic form
6
Q
draw a non-ionized form of an amino acid
A
grade yourself accordingly
7
Q
draw a zwitterionic form of an amino acid
A
grade yourself accordingly
8
Q
also known as side chain, which determines the identity and properties of an amino acids
A
R group
9
Q
have neutral hydrophobic side chain and include the aliphatic amino acids, located inside the amino acid
A
non-polar amino acid
10
Q
only nonchiral amino acid
A
glycine
11
Q
secondary, cylic, imino acid
A
proline
12
Q
aromatic amino acids
A
phenylalanine, tryptophan
13
Q
sulfur-containing amino acid
A
cysteine
methionine
14
Q
have neutral hydrophilic side chain particularly the amino acids, located outside the protein:
A
polar amino acid
15
Q
neutral hydrophilic polar amino acid
A
serine
threonine
16
Q
phenolic amino acid
A
tyrosine
17
Q
amide amino acids
A
asparagine
glutamine
18
Q
have polar and basic amino acid side chain which forms a positively charged ammonium group
A
positively charged amino acid
19
Q
example of postively charged amino acid
A
lysine
arginine
histidine
20
Q
have polar and acidic carboxylic acid side chain which forms a negatively-charged carboxylate group
A
aspartic acid
glutamic acid
21
Q
Glycine 3 letter, 1 letter
A
Gly, G
22
Q
Alanine 3 letter, 1 letter
A
Ala, A
23
Q
Valine 3 letter 1 letter
A
Val, V
24
Q
Leucine 3 letter 1 letter
A
Leu, L
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Isoleucine 3 letter 1 letter
Ile, I
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Cysteine 3 letter 1 letter
CYS, C
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Proline 3 letter 1 letter
Pro, P
28
Tryptophan 3 letter 1 letter
Trp, W
29
Phenylalanine 3 letter 1 letter
Phe, F
30
Serine 3 letter 1 letter
Ser, S
31
Threonine 3 letter 1 letter
Thr, T
32
Tyrosine 3 letter 1 letter
Tyr, Y
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Asparagine 3 letter 1 letter
Asn, N
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Glutamine 3 letter 1 letter
Gln, Q
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Aspartic acid
Asp, D
36
Glutamic Acid
Glu, E
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Lysine
Lys, K
38
Arginine
Arg, R
39
Histidine
His, H
40
draw cysteine
grade yourself accordingly
41
draw glycine
grade yourself accordingly
42
draw alanine
grade yourself accordingly
43
draw valine
grade yourself accordingly
44
draw leucine
grade yourself accordingly
45
draw isoleucine
grade yourself accordingly
46
draw proline
grade yourself accordingly
47
draw methionine
grade yourself accordingly
48
draw tryptophan
grade yourself accordingly
49
draw phenylalanine
grade yourself accordingly
50
draw serine
grade yourself accordingly
51
draw threonine
grade yourself accordingly
52
draw tyrosine
grade yourself accordingly
53
draw asparagine
grade yourself accordingly
54
draw glutamine
grade yourself accordingly
55
draw aspartic acid
grade yourself accordingly
56
draw glutamic acid
grade yourself accordingly
57
draw lysine
grade yourself accordingly
58
draw arginine
grade yourself accordingly
59
draw histidine
grade yourself accordingly
60
nonpolar amino acid interaction with water
hydrophobic
61
amino acid that Contain O and S atoms, but no charge
polar, neutral
62
Contain carboxylate groups, negative charged
polar, acidic
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contain ammonium groups, positive charge
polar, basic
64
Amino acids are also classified based on their nutritional requirements
essential
conditionally essential
nonessential amino acid
65
those that are not synthesized by the body and therefore must be obtained from diet
essential amino acids
66
essential amino acids
Histidine
Isoleucine
Leucine
Lysine
Methionine
Phenylalanine
Threonine
Tryptophan
Valine
67
considered essential under certain circumstances of conditions, synthesis limited in case of stress/starvation/disease
conditionally essential
68
example of conditionally essential
tyrosine
phenylalanine
69
can be made in the body, not needed in diet
nonessential amino acids
70
example of non-essential amino acids
Alanine
Asparagine
Aspartic acid
Glutamic acid
Arginine
Cysteine
Glutamine
Glycine
Proline
Serine
tyrosine
71
proteins with significant amounts of all essential amino acids
complete proteins
72
link amino acids with each other to form peptides and eventually protein
peptide bonds
73
condenses with another amino group of another amino acid
carboxyl group
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peptide bond is also called this
amide bond
75
side product of amine bond
h2o
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leftmost amino acid that has the free amino group
n-terminal end or terminus
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rightmost amino acid with the free carboxyl group
c-terminal end or terminus
78
process where water molecule is released
dehydration/condensation
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peptide bond has a ___ bond that joins 2 amino acids
covalent bond
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release of H2O
dehydration
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peptide bond has a ___ double bond character: as shorter than a single bond
partial
82
rotation around the bond is restricted because of this orientation
rigid and planar
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configuration of peptide bond where there is less steric hindrances of adjacent amino acid side chains
trans configuration
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peptide bond is charged what
uncharged
85
Polar H atom of N-H amino group has partial ____ charge and polar O atom of C=O carboxyl group has partial ____charge
positive
negative
86
Four reaction of amino acids
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
catalyzed by an oxidase or dehydrogenase enzyme where amine is removed and a-keto acid is formed
oxidative deamination
88
what is formed when amine is removed in oxidative deamination
a-keto acid
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Keto acid can be converted to what
glucose or ketone bodies
90
transfer of an amino group to an a-keto to form another amino acid
transamination
91
reaction takes place at alkaline pH and responsible for transfer of CO2 from the tissue to the lungs by hemoglobin
formation of carbamino compound
92
removes CO2 in amino acids to produces amines
decarboxylation
93
Amine formed in the decarboxylation process have ____ physiological activity
high
94
reaction happens in the presence of NH3 where the a-carboxyl group of an amino acid will react to form the amide
formation of amide linkage
95
happens in the presence of ammonia
formation of amide linkage
96
phosphate groups react with amino acids containing the hydroxyl group, -OH, to form phosphoproteins
ester formation
97
Happens in serine, threonine, tyrosine
ester formation
98
when an amino acid attaches to a carbohydrate
glycoside formation
99
reaction involves the amino acid cysteine when it forms disulfide linkages called disulfide bonds
reaction due to -SH group (disulfide bond formation)
100
involves the transfer of the methyl group of methionine to produce other biological compounds
transmethylation
101
formation of norepinephrine to epinephrine
transmethylation
102
important neurotransmitter that is synthesized from phenylalanine or tyrosine using hydroxylase and decarboxylase enzymes
dopamine
103
Binds to dopaminergic receptors and plays a role as a reward center of the brain
dopamine
104
Function in memory, mood, motivation, and control of movement
dopamine
105
deficiency in dopamine is associated with this, a progressive disorder that results to loss of muscular movement control
Parkinson's disease
106
Also associated with Hutington’s disease, schizophrenia, attention deficit/hyperactivity disorder (ADHD), and addiction
dopamine
107
dopamine made in what areas of the brain
substantia nigra
hypothalamus
ventral tegmental area
108
chemical messengers that your body can't function without
neurotransmitter
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molecules where neurotransmitter binds. Relay signal carried from one cell to another
receptors
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dopamine from this is released when receiving an award
ventral tegmental area
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dopamine released associated with movements and speech
substantia nigra
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the ventral tegmental area projects dopamine to the nucleus accumbens
mesolimbic pathway
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dopamine moves from the ventral tegmental area to the prefrontal cortex
mesocortical pathway
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dopamine projects from substantia nigra to caudate putamen nucleus
nigrostriatal pathway
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sends dopamine from hypothalamus to pituitary gland
tuberoinfundibular pathway
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more popularly known as adrenaline, the fight or flight hormone that is synthesized in the adrenal gland
epinephrine
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Released during stressful conditions or emergencies, creates the “adrenaline rush
epinephrine
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characterized by heartbeat elevation, increase in blood flow to the muscles, and blood sugar elevation by release of glucose from glycogen reserves
adrenaline rush
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Used in medicine for treatment of severe allergy called anaphylaxis and cardiac arrest
epinephrine
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Also acts as an excitatory neurotransmitter in a small number of neurons
epinephrine
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pair of endocrine glands found atop the kidneys
adrenal gland
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immediate precursor of epinephrine and is also known as noradrenaline
norepinephrine
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Both hormonal and neurotransmitter function
norephinephrine
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it is responsible for fight-or-flight response as in andrenaline
norepinephrine
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As a neurotransmitter, it increases libido or sexual arousal, heightens alertness and vigilance, and hastens memory formation and retrieval
norepinephrine
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dopamine, epinephrine, and norepinephrine are called this as they are derived from cathecol
cathecolamines
127
derived from amino acids phenylalanine or tyrosine
catechol
128
label the compounds and eznymes
grade yourself accordingly
128
important neurotransmitter that is synthesized from the amino acid tryptophan via hydroxylase and decarboxylase enzymes
serotonin
128
Synthesized in the gastrointestinal tract (GI) by the enterochromaffin cells for regulation of intestinal movements
serotonin
129
where 2 percent of serotonin was synthesized, playing a vital role in the regulation of mood, sleep, and appetite
central nervous system
130
where serotonin neurons are found
raphe nuclei
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6 families of serotonin receptors are what
g-protein coupled receptors
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1 family of serotonin receptors consist of
ligan-gated ion channels
133
naturally occurring tripeptide that has potent antioxidant property
glutathione
134
Become a popular ingredient in various whitening pills and cosmetic products
glutathione
135
glutathione amino acid
y-glutamylcysteinylglycine tripeptide
136
Most abundant non-protein thiol in mammalian tissues with millimolar concentrations
glutathione
137
Acts as a regulator of cellular redox state protecting cells from damage caused by lipid peroxides, reactive oxygen, and nitrogen species, and xenobiotics
glutathione
138
Important in key signal transduction reactions as a controller of cell differentiation, proliferation, apoptosis, ferroptosis, and immune function
glutathione
139
nonapeptide hormone and neuropeptide that is composed of Cys-Tyr-Ile-Gln-Asn-Cys-Pro-Leu-Gly-NH2
oxytocin
140
nonapeptide of oxytocin
Cys-Tyr-Ile-Gln-Asn-Cys-Pro-Leu-Gly-NH2
141
Produced in the hypothalamus and released by the posterior pituitary gland primarily during and after childbirth to stimulate uterine contractions and lactation
oxytocin
142
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
oxytocin
143
Available in injectable form for inducing child labor, and intranasal spray of psychiatric, hormonal, and even weight management
oxytocin
144
Produced in the hypothalamus and transported through axons to the posterior lobe of pituitary gland
oxytocin
145
ver of oxytocin may be involved with trust, empathy, and social bonding
centrally released oxytocin
146
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
vasopressin
147
nonapeptide of vasopression
Cys-Tyr-Phe-Gln-Asn-Cys-Pro-Arg-Gly-NH2
148
is also produced in the hypothalamus and released by the posterior pituitary gland but it functions as an antidiuretic hormone (ADH)
vasopressin
149
vasopressin is also known as
arginine vasopressin (AVO)
150
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).
vasopressin
151
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
vasopressin
152
