Biochemistry

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Total cards: 24•Content version: v4•Public deck•Updated: 8/1/2026

Card preview (24)

Front (Question)

Hydropathy index

Back (Answer)

measure of polarity of amino acid residue; how hydrophobic vs how hydrophilic an amino acid is

Front (Question)

higher the hydropathy value (kJ/mol) –> the more ______ the amino acid

Back (Answer)

hydrophobic

Front (Question)

lower the hydropathy value (kJ/mol) –> the more ______ the amino acid

Back (Answer)

hydrophilic

Front (Question)

hydropathy value of peptide chain

Back (Answer)

sum of individual hydropathy value of each residue

Front (Question)

primary structure of protein

Back (Answer)

sequence of amino acids, held together by peptide bonds

Front (Question)

secondary structure of protein

Back (Answer)

local folding, only relatively close residues interact, held together by backbone interaction (H-bonds between amine H and carbonyl O of the backbone)

Front (Question)

tertiary structure of protein

Back (Answer)

global folding, held together by side group interaction (disulfide bonds, ionic bonds, H-bonds, hydrophobic interaction)

Front (Question)

quaternary structure of protein

Back (Answer)

different peptides/proteins interacting, held together by side group interactions

Front (Question)

forms of denaturation

Back (Answer)

heat, pH, salts, detergents

#10

Front (Question)

Lineweaver-Burke Plot: Equation

Back (Answer)

#11

Front (Question)

Lineweaver-Burke Plot: x-intercept

Back (Answer)

#12

Front (Question)

Lineweaver-Burke Plot: y-intercept

Back (Answer)

#13

Front (Question)

competitive inhibitor

Back (Answer)

binds E, Km increases, Vmax stays the same

#14

Front (Question)

uncompetitive inhibitor

Back (Answer)

binds ES, Km decreases (more ES formed), Vmax decreases

#15

Front (Question)

noncompetitive inhibitor

Back (Answer)

binds to E and ES, Km stays the same, Vmax decreases

#16

Front (Question)

allosteric inhibitor

Back (Answer)

binds to a site other than the substrate binding site

#17

Front (Question)

bind to a specific amino acid in the active site

Back (Answer)

group specific reagents

#18

Front (Question)

similar size and shape as substrate, binds covalently in active site

Back (Answer)

affinity labels (substrate analogs)

#19

Front (Question)

very similar to substrate (in size, shape, and charge), bind in active site with noncovalent bonds, causes reaction to happen, product is made that covalently binds to active site (blocking it)

Back (Answer)

suicide inhibitors

#20

Front (Question)

amino acids found in active sites

Back (Answer)

catalytic residues

#21

Front (Question)

types of enzymes

Back (Answer)

OTHLIL: oxidoreductases, transferases, hydrolases, lyases, isomerases, ligases

#22

Front (Question)

optimal pH and temperature of enzymes

Back (Answer)

optimal pH varies greatly, temperature is 37 ºC

#23

Front (Question)

the non-protein component of an enzyme required for catalysis, some enzymes require them but not all; two types: essential ions and coenzymes

Back (Answer)

cofactor

#24

Front (Question)

type of cofactor: organic molecules that contribute to catalytic function of enzymes; include NAD+/NADH

Back (Answer)

coenzymes