quicksheets biochem Flashcards
L - chiral amino acids
all except glycine, which isn’t chiral
S - conformation amino acids
all except cystein
nonpolar, nonaromatic AA
gly, leu, ala, met, val, ile, pro
positively charged AA
arg, lys, his
negatively charged AA
asp, glu
polar AA
ser, thr, cys, asn, gln
aromatic R groups AA
trp, phe, tyr
primary structure
linear sequence of AA
secondary structure
alpha helices, beta sheets, stabilized by hydrogen bonding
tertiary structure
3-d structure stabilized by hydrophobic interactions, acid-base interactions (salt bridges), hydrogen bonding, and disulfide bonds
quaternary structure
interactions between subunits
denaturation
caused by heat and solutes
enzymes
lower activation energy w/o changing free energy (delta G) or enthalpy (delta H); change kinetics
ligase
joins two large biolecules
isomerase
interconvert isomers
lysase
cleaves w/o addition of water or electron transfer
hydrolase
cleaves w addition of water
oxidoreductase
catalyze redox rxns involving transfer of electrons
transferases
move functional group from one molecule to another
saturation kinetics
as substrate conc. increases, rxn rate also increeases until max rate is reached: v=vmax[S]/(Km+[S])
one-half vmax
[S]=Km
competitive inhibitor
binding at active site, increases Km, no change to vmax
noncompetitive inhibitor
binding at allosteric site, no change to Km, decreases vmax
mixed inhibitor
binding at allosteric site, can increase or decrease Km, decreases vmax
uncompetitive inhibitor
binds at allosteric site, decreases Km, decreases vmax
structural proteins
fibrous, including collagen, elastin, keratin, actin and tubulin
motor proteins
capable of force generation through conformational change; myosin, kinesin, dynein
binding proteins
bind a specific substrate, either to sequester it in the body or hold its concentration at steady state
cell adhesion molecules
bind cells to other cells or surfaces; cadherins, integrins selectins
antibodies (immunoglobins, Ig)
target specific antigen, which may be a protein on surface of pathogen or a toxin
ion channels
can be used for regulating ion flow in or out of a cell, including ungated channels, voltage-gated channels, and ligand-gated channels
enzyme-linked receptors
participate in cell signaling through extracellular ligand binding and initiation of second messenger cascades
G protein-coupled receptors
have a membrane-bound protein associated with a trimeric G protein; they also initiate second messenger systems
triose, tetrose, aldose, ketose
3 carbon sugar, 4 carbon sugar, sugar w aldehyde as most oxidized group, sugar with ketone as most oxidized group
D-sugars
-OH on the right
L-sugars
-OH on the left
diastereomer
differ at at least one, but not all, chiral centers; epimers differ at exactly one; anomer type of epimer
cyclization
ring formation of carbohydrates from their straight-chain forms
anomeric carbon
new chiral center formed in ring closure; it was the carbon containing the carbonyl in the straight-chain form
alpha anomer
have the -OH on the anomeric carbon trans to the free -CH2OH group
beta anomer
have the -OH group on the anomeric carbon cis to the free -CH2OH group
mutarotation
one anomeric form shifts to another, w the straight-chain form as an intermediate
monosaccharides
single carbohydrate units that can undergo oxidation-reduction, esterification, and glycoside formation; fructose, glucose, galactose, mannose
disaccharides
sucrose, lactose, maltose
cellulose
main structural component of plant cells walls; main source of fiber in human diet
starches
amylose and amylopectin; main energy storage for plants
glycogen
major energy storage form for animals
nucleoside, nucleotide
5 carbon sugar bonded to nitrogenous base; w phosphate group(s) added
Chargaff’s rule
purines and pyrimidines are equal in number in a DNA molecule; amount A=T, G=C
histone proteins
DNA is would around H2A, H2B, H3 and H4, to form nucleosomes, which may be stabilitzed by another histone protein H1