Biochem quiz 1 - Amino acids Flashcards
Acidic Amino acids
Apsartic acid, glutamic acid
non polar alipathic AA
glycine, alanine, valine, proline, leucine, isoleucine
branched non polar alipathic AA
leucine, isoleucine, valine
Polar uncharged AA
serine, threonine, aspargine, glutamine
sulfur containing R group
methionine, cysteine
Negatively charged AA R group
glutamate, aspartate
Positively charged R group
Histidine, lysine, Arginine
aromatic AA
tyrosine, phenylalanine, tryptophan
which substances have L configuration?
Amino acids
Which substances have D configuration?
all sugars metabolized in the body, such as ribose , have D configuration
zwitterion
neutral molecule with a positive and negative charge
NO NET CHARGE
isoelectric point
point at which there is no net charge
if ph is less than 2 for pk1, what charge will exist?
+1
if ph is greater than 10 for pk2, what charge will exist?
-1
how do you solve for the PI?
average of the two ionizable groups of an amino acid
Abbreviations of AA’s

post translational modification to proteins, types:
carb addition, lipid addition, regulation, modfied AA
what is phosphorylation, what AA take part in this?
OH side chain required, Serine, threonine, tyrosine
adds hydroxyl group , phosphate group gets added. adds negative charge, Kinases add phosphate groups.
acetylation
NH2 of lysine terminus
proteins that bind to DNA
ADP ribosylation
N of Arg, gln, S of cysteine
Modified amino acids : Oxidation
lysine, proline
Modified AA Carboxylation
glu
chiral
4 different substituents , rotate polarized light, ALL chiral AA’s are of the L configuration
which AA does not have a chiral center?
Glycine, 2 H side chains
When carb. acid loses a proton it becomes_____ charged.
Negatively charged, increasing PH, therefore, - charge. If ph decreases, gaining protons. If pH increases. losing protons.
Acids want to donate protons, become more ACIDIC
When Amino group picks up a proton, it becomes _____ charged.
positive . Gaining more H protons, decreasing pH
Bases want to gain/accept more protons, become more Basic.
basic vs acidic
base- proton acceptor
acid- proton donator
What is the best type of buffer? What pH/pka?
The best buffer is when the pH is closest to the pKa
post translational modification helps to do what?
Anchor proteins to the membrane
lipid chains , what is on inside and outside?
polar chains on outside, greasy acyl chains on interior
Role/ importance of Disulfide bonds
link cysteine molecules together
link peptide hormones together in the blood
What tool is used to detect AA’s?
Chromatography
AA absorb UV light, higher peak means more of a certain AA, changes in levels of AA can help detect disease
proline is an_________ acid
IMino
ionizable group pka’s
acidic AA
around 4. for aspartate and glutamate
pKa for arganine and lysine:
12.5 and 10.5
pka for histidine
6
pka for cysteine and tyrosine
8.4 and 10.5