MCAT UWorld Flashcards
Catalytic efficiency
Kcat/Km
measure of how quickly an enzyme CATALYZES a reaction at LOW SUBSTRATE concentrations
catalytic turnover (Kcat)
rate at which enzyme-bound substrate is converted into product
describes rate-limiting step of catalysis under saturating conditions of substrate
Isoelectric point (pI)
pH at which protein has a net charge of zero
ambient pH < pI
protein gains protons (protonates) and becomes POSITIVELY charged
- rich in high pKa amino acids
ambient pH > pI
protein loses protons (deprotonates) and becomes negatively charged
- rich in low pKa amino acids
Enantiomers
molecules with the same molecular formula that are mirror images because they differ in the orientation of every stereocenter
- nonsuperimposable mirror images
- same physical and chemical properties
- can be separated by column chromatography as either R or S still interact with the chiral stationary phase more strongly
Most biologically relevant sugars adopt the __-configuration sugar
D-configuration
glycosidic bond
bond between the anomeric carbon (the hemiacetal or hemiketal) of a carbohydrate and any other biological molecule, including proteins, lipids, nucleotides, and other carbohydrates.
structural lipids
hydrolyzable glycerophospholipids and sphingolipids, nonhydrolyzable cholesterol
lipids primarily responsible for energy storage
triacylglycerides (metabolized through hydrolysis and beta-oxidation)
Fatty acid structure and membrane fluidity
nonpolar hydrocarbon chain + polar carboxyl head group
short tails -> fewer intermolecular interactions => INCREASED fluidity
higher # of double bonds -> decreased IM interactions => INCREASED fluidity
cis double bonds -> INCREASED fluidity because they’re less tightly packed
Short unsaturated fatty acid chains have the GREATEST fluidity
Long saturated fatty acid chains have the LOWEST fluidity
unsaturated fatty acid chain
double bond (cis C=C) that creates kink or bent, which INCREASES fluidity
pyrimidines
1 ring: C and T/U
T = one hydrogen bond acceptor (O) and one hydrogen bond donor (NH)
C = two hydrogen bond acceptors (O and N) and one hydrogen bond donor (NH2)
purines
2 rings: A and G
A = one hydrogen bond acceptor (N) and one hydrogen bond donor (NH2)
G = one hydrogen bond acceptor (O) and two hydrogen bond donors (NH and NH2)
Prostaglandins
act as autocrine and paracrine signals to produce localized inflammatory response
phospholipase enzymes -> arachidonic acid -> modified to form prostaglandins (20-carbon nonhydrolyzable lipids)
autocrine signaling
act on the same cell that secreted the signal
signaling and target cells are the same or similar
paracrine signaling
target cell is near the signaling cell, act on cells in local area
juxtacrine signaling
signaling cell directly stimulates receptor of adjacent target cell
endocrine signaling
hormones travel through the bloodstream to distant areas (e.g. organs)
catecholamines
i.e. epinephrine and norepinephrine: hormones derived from tyrosine
- short-term stress
- endocrine signals
ketone bodies
fuel sources produced under LOW glucose conditions
- derived from acetyl-CoA
terpenes
precursors of synthesis of cholesterol and steroid hormones, derived from isoprenes
Lineweaver-Burk plot
1/V0 = (Km/Vmax)*(1/[S]) + 1/Vmax
slope = Km/Vmax
y-intercept = 1/Vmax
x-intercept = -1/Km
Cation exchange columns
Contain resins w/ negatively charged residues, which bind positively charged molecules (cations) -> buffer gradually changed by increasing pH and/or salt concentrations. As the pH rises, protons are removed from bound molecules, causing molecules to lose positive charge and eventually ELUTE. Similarly, cations in the salts added to the column w/ the bound cationic molecules, displacing them from the column.
To bind the column in the experiment, all the amino acids must initially have a net positive charge by fully protonating all amino acids -> by bringing pH BELOW THE LOWEST PKA of all the amino acids present.