biochem things i need to know

negative is

acid

positive is

basic

a amino

phi

a carb

psi

a helix

every 3.6 turn

his tag has an affinity with

metal

ph < pka

multiple H

ph > pka

no H

motor involves

atp

road involves

gtp

holoenzyme

complete, function enzyme

apoenzyme

inactive enzyme

trypsin cleaves after

k and r

asp 52 involves what

covalent bond

glu 35 involves what

acid/base

when you see nad/nadh think of

oxioreductase

atp usually involves

ligase

Oxidoreductase

moves electrons or hydrogen, look for NAD⁺/NADH or FAD/FADH₂.

Transferase

transfers a group, especially a phosphate or amino group.

Hydrolase

uses water to break a bond.

Lyase

breaks or forms a bond without using water. (pi bonds)

Isomerase

rearranges atoms within the same molecule.

Ligase

joins two molecules together, usually using ATP.

what do his ser and asp have in common

catalytic covalent bond

km is half of

vmax

highest mm is

lowest affinity

alters both km and vmax?

uncompetitve

atcase is

allosteric

carbamoyl uses

tunnel

omp is

proficient

t state has

inhibitors

r state has

acvitavors

sertine and cystine are

self starters

aspartyl metalloproteases are

water users

hemoglobin

transport, four units, hemo

myoglobin

storage, holds onto oxygen, single protein subunit

distial histidine

dodoes not bind to iron, prevents realease of oxygen species

cell buffering uses

imadazole

L config involves

nh2 on the left

pyruvate gets turned into

alanine

oxoloacetate gets turned into

aspartate

a ketoglutarate gets turned into

glutamate

what is a peptide plane

ca c o n h ca

antiparallel is

straight

parallel is

crooked

if reduing agent is removed before urea

disulfide bonds not positioned correctly

in sds the proteins move towards

the positive electrode

in gel filtration it separates by

native states

collagen needs what

hydroxylated proline

a tubulin involves

globular bidning for GTP

TTrypsin needs what triad

Ser his asp

enzyme affects what

reaction rate

lower km is

higher affinity

perfect enzyme is

in between 10^8-10^9

sigmoidal is

allosteric with multiple sites

serine tried

ser his asp

heme iron is

6 coordination sites

sickle cell is what

glu-val mutation in b chain

linpinskis rule does not include

cost

sildenahil targets

phosphoidis

aspirin targets

protesglandin h2

Why does violet light make a cell glow green?

Violet light gives electrons energy, and when they lose that energy, they release green light.

More energy → shorter wavelength

blue/violet

Less energy → longer wavelength

green/yellow/red