Summary Biochemistry – Complete Study Notes (Amino Acids, Enzymes, Metabolism, Protein Structure) – Comprehensive Exam Material

B branched sheet
Amino Acids : all are 2/(5) config.
↑
Glycine G Valine V Isoleucine I
Anne
A ne -




TH3 TH3 TH3
⑪- - ⑰
- ⑭- -o
L



Proline P MethionineM NONDOLAR W Tyroprophan IP
-

TH3
TH3
TH- (HYDROPHOBIC)
Q-




-
C ⑪ --

-
, Leucine L ⑰
L
-




NH3




T
F Gamma
thenylalan
e
Branched



⑰ C-c-e
-




-
CAN FORMEDE BONDS
Sermine S
↑ C
Cysteine .
confi
TH3 Threonine Y -




TH3
-




⑰ -H TH3 Asparagine N
⑭- -SH
- ⑪- XoH THE N


GLN Glutamine Q
-




Ths o
-
O Tyrosine

TH3
Y

H -
-I
NH2 POLAR ⑪ -

-c
ko CHYDROPHILLIC) to
·

, (f)


I
D E
Aspartate o utamate
NH3
⑳
⑪ c - co ④- c c c
b
- - - -




" "
- -
d
↳sineK HRK

TH3 (t)
Q -

C-c-c-c-- B
- A
Arginine
-
R (HGHPI) S
TH3
I

- C


Histidine H
- >
-
phosphorylation
TH3


&
> Ketogenic
-

,site
arectedeness
f caster
1ry structure :



hydrolysistogether
Val / ASp1 Glu /HIS -PEPTIDEBOND
sub.cmsAt] ,
2ry structure :
[Nucleophilic cylEnergehcFavorable Stable : RESONANCE
Stabilization
CAMIDES)
208a-helix (Keratin) a partial double
- Hydrogen bond bond character
M Bpleated (fibroin) (blw AMIDE PROTONS +
CARBONYLOXYGEN)


zry structure "denaturation" :




ThyrophonyerpentropyspontaneS
n
care

Salt Bridges Con pair) -
> Vaw , hydrogen bond,
Disulfide S-S
louk bond




Si
ury structure :




↓↓ S . A
- > ** Stability
↓↓ amt of DNA coded

J
multmeric protein
.




↓ ↓ distance > ↑↑ speed -

faster
* cooperativity "multiple subunits


·
CONVALENT 2/ nucleophilic a d
occurs .
:

"Salman than can threat YOU"
serine , threonine , Cysteine , Tyrosine Lysine
,
S + C Yk

, cenzymatic reaction)
·
Entropic Penalty : unfavorable interacti .




denature : >
-
HYDROPHOBIC + HYDROPHILLIC
> Temp
-




- ↓ pH
eadd Concentrated chatropic
·
agent

Enzymes :




AFFECT GiBBs) -
> affect TEMP rxn9tEa
biological Catalyst (DON'T (a rate
ENZYMES : .
of


useofactors "transfer functional
1) Oxireductases >
- 2) Transferases -> Kinases group"
↳ Transaminatio
O
↓ =
Aminotransferases




I
cam of Loss of O
·
transfer of amino group- > Ketoad

Losso T GainOT
e- acceptor OXIDANT
= e-donor REDUCTANT
=
Glutamate
↳ minotransferases
-
keoglutation
NO 2 PRODUCTS
>
(Only 1)
-




3) Hydrolases 4) Lyases



- ·
· S
X +
H20ylases Rece upX
ind
-


breakdown
&
lipase , peptidase, nuclease, phosphatase
↳ ·
protease HYDROLYZE AMIDE
:



PROLASE
6) Ligases
BONDAme as
5) Isomerases
Addition (synthesis) reaction
x -X y -y
Constitutional somers DNALIgases ADNA
Steroomers




·
CONDENSATION :
LEAVE H20
·
HYDROLYSIS : CONSUME H2O
- -




i Endonuclease -> Cuts Within nucleic acid (entical for DNA repair)
I
Exonuclease -
> removes nucleotides (3-5)
D Ribonuclease -
>
degrades RNA (reverse transcription)

, rate limit t
vo-vo-m---man
chaels-Mentes



Step

↑
Kmdating Umaxofenzymes turnover max
kat =
Etot
·
phosphorylated IS FASTER than Unphosphorylated


catalytic eff
= What binding affinity



Substrate affinity

#max
Keat &




Vmax[# of enzymes #induction
M
kmdanity #upregulat




enzymes
Uma
↑No
↑ Vmax


one
# activation
numb .
of
Potentiator!
&*
J HIGH Kat
CONTROL




-
affinity




i fo
S⑭ ↓↓ Vmax
High
] cow
Kcat
↓ ↓ numb. Of enzymes

repression
downregulation
desensitization
~
#
noncompetitive O
Vo Vmax
=
(ims)
low cat. effici .
Vo =

maxsa
&
[S]


Hill coeff .
>
-




Glysodic bond : Irrevesible ·
Of 1 NEGATIVE
* y Cooperativity
[convalent bond] ·
It POSITIVE