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