BC - unit 2 Flashcards
___ ___ is a monomeric unit of peptides and proteins
amino acids
most amino acids occur as __-__ ___ ___
L- alpha amino acids
10 essential amino acids
phenylalanine valine threonine tryptophan isoleucine methionine histidine arginine leucine lysine
3 letter abbreviation of phenylalanine
phe
3 letter abbreviation of valine
val
3 letter abbreviation of threonine
Thr
3 letter abbreviation of tryptophan
trp
3 letter abbreviation of isoleucine
Ile
3 letter abbreviation of methionine
Met
3 letter abbreviation of histidine
His
3 letter abbreviation of arginine
Arg
3 letter abbreviation of leucine
Leu
3 letter abbreviation of lysine
Lys
acronym for essential amino acids
PRVT TIM HALL
what two essential amino acids can adults synthesize but babies and kids cannot?
Histidine
Arginine
12 non-essential amino acids
glycine alanine serine tyrosine cysteine aspartic acid asparagine glutamic acid glutamine proline hydroxyproline hydroxylysine
what two non-essential acids are not required for protein synthesis?
hydroxyproline
hydroxylysine
5 aliphatic amino acids
Glysine alanine valine leucine isoleucine
5 hydroxyl amino acids
serine threonine tyrosine hydroxylysine hydroxyproline
2 sulfer amino acids
cysteine
methionine
3 carboxyl/amide amino acids
aspartic acid
glutamic acid
asparagine
4 basic amino acids
lysine
arginine
histidine
hydroxylysine
4 aromatic amino acids
histidine
phenylalanine
tyrosine
tryptophan
2 Pyrrolidine amino acids
proline
hydroxyproline
phenylalanine is used to make ___
tyrosine
____ is an intermediate of the sulfur –> methianine
homocysteine
__ functions with vit B12
homocysteine
high levels of homocysteine is associated with ____
atherosclerosis
___, __, ___ is used to try and counteract homocysteine to make more cysteine and methianine
B6, 9, 12
___, ____, ___ ___ are intermediates in biosynthesis of urea
ornithine
citrulline
arginosuccinic acid
_-___ used as a drug for parkinsons disease
L-DOPA
L-DOPA is a precursor for biosynthesis of ____
catecholamines
3 of the most abundant catecholamines
epinephrine
norepinephrine
dopamine
all catecholamines are produced by ___ and ___
phenylalanine
tyrosine
____ –> tyrosine –> L-DOPA (catechol) –> dopamine (catecholamine) –> NO LONGER AN AMINO ACID –> norepinephrine –> epinephrine
phenylalanine
phenylalanine –> ____ –> L-DOPA (catechol) –> dopamine (catecholamine) –> NO LONGER AN AMINO ACID –> norepinephrine –> epinephrine
tyrosine
phenylalanine –> tyrosine –> _____ (___) –> dopamine (catecholamine) –> NO LONGER AN AMINO ACID –> norepinephrine –> epinephrine
L-DOPA (catechol)
phenylalanine –> tyrosine –> L-DOPA (catechol)–> ___ (____) –> NO LONGER AN AMINO ACID –> norepinephrine –> epinephrine
dopamine (catecholamine)
phenylalanine –> tyrosine –> L-DOPA (catechol) –> dopamine (catecholamine) –> ___ ____ ____ ___ ___ –> norepinephrine –> epinephrine
NO LONGER AN AMINO ACID
phenylalanine –> tyrosine –> L-DOPA (catechol) –> dopamine (catecholamine) –> NO LONGER AN AMINO ACID –> ____ –> epinephrine
norepinephrine
phenylalanine –> tyrosine –> L-DOPA (catechol) –> dopamine (catecholamine) –> NO LONGER AN AMINO ACID –> norepinephrine –> ___
epinephrine
thyroid hormone is deried from ___
tyrosine
tyrosine is a precursor to ___
thyroxine
2 precursors of thyroid hormone
3 - monoiodotyrosine
3,5 - diiodotyrosine
thyroid hormone does 3 things
increases basal metabolic rate
protein synthesis
cell proliferation
hyperthyroidism
too much thyroxin
increase BMR
increase BMR causes
weight loss more heat sensitive to heat sweating anxiety flushing
T4 is ___ abundant than T3
more
T4 is ___ active than T3
less
_-____ is part of pantothenic acid (Vit B5)
beta-alanine
___ is part of taurocholic acid (bile acid)
taurine
-chol
cholesterol
bile acid is based off ___
cholesterol
___ helps with integrity and function of the retina
taurine
___ is an inhibitory neurotransmitter from glutamate
GABA
___ ___: when the 4 groups on a carbon are different
chiral carbon
chiral carbon can deflect ___ ___
polarized light
chiral carbons that deflect light to the left are ___ also by __ or __
levorotatory
l
-
chiral carbons that deflect light to the right are ___ also by __ or __
dextrorotatory
d
+
____: a molecule which possesses both positive and negative charges
zwitterion
at low pH there will be ___ (+) charge
more
at high pH there will be ____(-) charge
more
lot of H+ around ___ and ___ are favored
NH3+
COOH
low pH: there is lot of ___ in the solution
H+
if [COO-] is equal to [COOH] then the ration of [COO-]/[COOH] is equal to ___
one
is the acid form equals the base form then the pH is ___ to the pKa
equal`
if R-groups are hydrocarbons –> ___
hydrophobic
hydrophobic amino acids can form ____ bonds
hydrophobic
___ bonds: association between hydrophobic compounds
hydrophobic
if R-groups are polar then they are ___
hydrophillic
hydrophilic amino acids can form ___ or ___ bonds
ionic or hydrogen
if R groups are aromatic they have strong ___ absorption
UV
if R groups are -OH they become esterified by ____
PO4
phosphorylation alters ___ function
protein
if R groups are SH they can oxidize to form __ bond
disulfide
if R-groups are SH they maintain a ___ structure
tertiary
___ bond is between COOH and NH3
amide/peptide
disulfide bond is usually formed between two ___
cysteines
disulfide bonds are involved in __ reactions
redox
if R groups are OH or NH2 they can form ____ by covalently bonding carbs in ___ bonds
glycoproteins
glycosidic
peptides have ___ than 10 amino acids
less
polypeptides have __ than 10 amino acids
more
proteins have ___ amino acids and can be comprised of many ___
many
polypeptides
amino terminal are always on the ___
left
carboxy terminal are always on the __
right
____ is an intracellular antioxidant
glutathione
glutathione prevents ___
oxidation
___ can reduce back to what it was before oxidation
gluthione
if redox happens then ___ has to happen somewhere and vis versa
oxidation
____ _ is a pain neurotransmitter
substance P
___ _ is an 11 amino acid peptide in gut, spinal cord and brain
substance P
___ are vasodilatiing amino acids that are derived from proteolytic cleavage
kinins
____: analgesic action like opiates
opiopeptides
3 opiopeptides
enkaphalins
beta-endorphin
dynorphin
ALL HAVE -in
enkaphalins are ___
pentapeptides
beta endorphin is a ___ amino acid polypeptide derived from ___
30
lipotropin
___: an opiopeptide in the spinal cord
dynorphin
primary structure of proteins are connected by ___ bond which can be hydrolyzed by ___ or boiling
peptide
proteases
primary structure is dictated by ____ in the ___
codons
genes
primary structure dictates ___ organization
subsequent
4 forms of secondary structures
alpha-helix
beta-pleated sheet
beta-bending
random coil
alpha-helix is like a ___ ___
spiral staircase
beta-bending has a particular ___
kink
random coil provides ___
elasticity
alpha helix and beta pleated sheets have ___ bonding between amino acids
hydrogen
tertiary structure that have 4 types of bonds
hydrogen
ionic
hydrophobic interactions
disulfide
quaternary structure is when 1 3D protein is linked with a ___
second
quaternary structure have 3 types of bonds
hydrogen
ionic
hydrophobic interactions
hemoglobin are a ___
hemoprotein
adult hemoglobin HbA are written out
alpha 2 beta 2
fetal HbF are written out
alpha 2 gamma 2
__ right handed alpha helices in each alpha subunit
8
__ right handed alpha helices in each beta subunit
7
functions of hemoglobin
O2 and CO2 transport
buffer
hemoglobin acts to neutralize huge ___ differences
pH
what binds O2 (3)
iron
histadine (F8)
histadine (E7)
histadine (E7) prevents
CO binding
R form of hemoglobin binds ___ and T form ___ and binds ___
O2
cannot
CO2
cooperative allosterism
binding of 1st O2 takes the longest, the rest get progressively faster. bc binding O2 changes conformation of other subunits, facilitating further O2 binding
myoglobin is a ___
hemoprotein
myoglobin has ___ polypeptide of 153 amino acids
1
myoglobin has ___ right handed alpha helices with heme between helices E and F
8
O2 bound to myoglobin is a reserve for when ___ of tissues is low… it is then released for ___ synthesis
pO2
ATP
most abundant protein in the body
collagen
mature ___ is composed of 3 alpha carbon chain subunits
tropocollagen
___ is the most abundant amino acid in collagen, with lots of ___ and ___
glycine
proline
lysine
collagen synthesis:
mRNA to ___ chain
pro-alpha
collagen synthesis:
hydroxylation of pro-alpha chains
- proline by ___ ___
- lysine by ___ ____
prolyl hydroxylase
lysyl hydroxylase
Collagen synthesis:
hydroxylation of proline and lysine require 3 things
vitamin C
Iron
O2
collagen synthesis:
3 hydroxylated pro-alpha-chains H bond to form __-___
pro-collagen
___ ___: genetic mutation where gly is replaced by ___
cysteine
collagen synthesis:
secretion of pro collagen out of cell by ___
exocytosis
cleavage of N and C terminal segments by procollage peptidases –> ____
tropocollagens
oxidation of some lysines to ___ ___ by ___ ___ and requires 3 things
lysyl aldehydes lysyl oxidase copper vit B6 O2
____ due to defiiciency of lysyl oxidase
lathyrism
___ formed from condensation of 3 lysine aldehydes + 1 unmodified lysine
desmosine
desmosine is the marker of ___ ___
elastin metabolism
rigor mortis happens bc of lack of ___
ATP
water soluble proteins are ___
albumins
dilute salt solution proteins are ___
globulins
acid/base soluble proteins are ___
glutelins
acid/salt soluble proteins are __
basic proteins
globular proteins
most belong here
fibrous proteins
elongated
actin, myosin, collagen, elastin, keratin
___ proteins: no attachment of non-protein component
simple
___ protein: apoprotein + prosthetic group = holoprotein
conjugated proteins
apoprotein is a __ protein
naked
5 conjugated proteins
hemo glyco lipo phospho metallo
