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
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
