AVLINO
ACIDS
PROTEINS
ENZYME
--
in troductionto proteins
functions immnnoalobnlín
G
-
act astoxin, antibiotics andvatines 1500
amino
acidslong
protein stuncture
VanderWaals
Atom
with
representation
Surtale
represent
colouys
Surface
and
pydtein
=
representation
of : looamino
thesurface
Show alid
biQ protein
lysozÿme
diagram ribbon or
cavtoon
secondavy showthestynctnye proter of
henices
alpha
beta sheets
nighly
internution
resrstance
thermaistable,
withneighboring
todenaturation
torstability require
styands
-
mod
el spacetilling
atoms
them
,fimthespacebetween
representsmolecmie a
0freiative
byShowing sizes n
ball -and- Stick model
ntoms
connected
by stiuksshow
bonds atoms
andangiesbetween
aminoacids / STA
amine carboxyl
chainRsíde
backbone
peptide
primary N
amine cayboxylicaüid
'COOT
-
H alphacarbon
( chiralcenter)
number =
A1foursitesare bydifferent
occupied
20chival ( ne
centers)
amino
groups
number
aud
ofform
is Asymmetyic.
S+ereoisomers
, ,
formpolypeptides peptide
bymaking bond
as
reaction, prodncesH2d
by -product Condensation
peptide
c Hz R -H:0
R 0 bond R
Il
NH: coo * NHS- c COD NH31- N C CD0
H H H H H
peptide bond
covaient >strongesttupeof moieuniar
bond bond
chavacter
partialdouble
bondnas
rigid as
it A
..
...•-
0...0.
cis
H
trans isomerisation
0-
H
==
C- N bond 1.32 A
normalC-Nbond I-4QA
bond CEN 1.27A
1enqthshorter
more
viqia
bond
Z
H
TYAnS Cis
stable more ©olivia_liying
,aminoacid
U
chivality
mirvor image
#412/092CA0/1V
molecule
D- (somer and L-isomer
identify nsingCORN
is non
rmie
COoH
doJ H
on -
its achiral
Superimposable
COOH
H
left to right to
NH2 R NHZ
--
Levorotary L
steredisomer DextrorotatoryDStereoisomer
nre
abletotwisttheangieofpolarisedlight
steredisomers
right, L isomer turnsporarisedlight to D
toleft isomer
isomeris a nature seletted asummetricisomer
in mammAls
L
only arefoundin proteins
Lisomer
thalidomide
Rlrignt) thalidomide
babyNON.Te
was
for
prescribed
fof scieft) thalidomide
nansea
duringpregnanty
in
preventlimbdevelopment
teratogenic,induce birthdetects
D-serine
systemand
azwitterion
forms
íonsaISoknown
are
D-asparate
ataspeciticpHknown
asdipolar
mn
found
asrsoelectril
nervous
centval systemand
poínt pI
endoerine
,
chargehave
nentralnet NUNR
amino
aud
buffers aroup
carboxyi acts
and duetothepresence
ofamino
H3N COSH H3N COD H2N C0D
qlyciniumcation glycine Zwitterion alucinateanion
PH pI pH PL PHZPI
nentrainetcharge
=
alidic bAsil
H H
O
H* 2 =
Lnal bufferina N-H
•
regions
H*
H 0H
primary amine carboxylic audcarboxylate
©olivia_liying
, -
nonpolar
H3N*=
C Coo
H
- C
CHJ CH
CH3CHS
C
CH2 HaC CH
SH CH2
H
HaN-C --coO
cHa
-
Alanine Valine Cysteine Proline Phenylalanine
Gyeine A P FHM
.••.
core
pydtein +buried(nside
C 0- C amino
non-polar acids011
avehudrophobic
H3 C CH CH2 CH2 inclndes
cysteineand
tryptophan
-É
0-5-5
CH2 CHa
1Argest tryptophan
CH3CH3 CH3
D- : glycine
smailest
CH3
Lencine Isolencine NVANmethionine Tryptophan
Itigdedd M W
polay
0-0- 8-0- 2-=1
CHa
OH OH CH3
OH NHZ0
NHZ O
Serine Threonine TyrosineAsparagine Gintamine
S N Q
t charge(basic) chargel acidic)
charged
amines C
NH 0
CH2
AHT
Histidine C
Pua
CN
S-E_É_A
MNA 04°
0 0
1
NHgt C=-NHS
NHZ
Lysine Ar qinine©olivia_liying Aud
Glutamic
AsparticAuid
K R D E
, Glucine
its sidechainsmall(H) ASiS flexible yotataole peptidebond are
nenrotransmitter
forms by Rgromp
%restrilted lextept glytine)
andhasnoD ¡Somer
qroups carbon)notan
avound 3
opticalisomer-(onm
Cysteines
athiolqvoup
has
cantoother
bond + toform
custeine bond
bydisuiphide
cystine
a+2H 20-
HOOCCHCH2S-SCH2CHCOOH
cystime work
outside to
of theproteinsthathave
>oxrdation intreasecen
nse to
disulphide bond
NHa drsuiphide NH2 losee- Stability
-- -
bond insulin
0 pepsin
proteinsmetals to (h
binds phospholipase venom
dee
NH3* NH3° Znit
Coo C CH2 SH *t coo~- C CH2
NHqlt
H H
more easily likelosthydroxyl(-0H). H1S
Histidine
basic
1owpH +Chorge
hign pH: nentyal
acceptsHtbelow
nentralpH
Side tophysiological
pKaClose PH duetoits chain,imidazole
ring, histidmnea(1.4)
has
can
existinbothnentraland posrtive
charge
-
to PHchanges,switch
auditysensitive
surrounding stateaccordingto
-
Strongly
metalsbindsto
n0tin human
charged
Zn>t H1 H
CH2 C CDOH
NHz.
poly histidine
ta0isnsefmi
forproteinpuvification
precursor
for histamine SNINOSINT
converSion tohistamine
histidine
AromaticAminDacids
byhistidme
decarboxylase
absorb
lignt
diet essentialin human
phenulketonuia phenyimanine
hydrbxylase
excess
down inability tobreak phenylaianine Atyrosine
phenylalahine
treatment
10W
Phediet theproduction
tyrosineis needed
for
avoidsaspartameavtifruial
sweeteners of nenvotransmitters
aspartit auid phenyialanine untreated
PKuleadto intenetnal
disability
©olivia_liying
ACIDS
PROTEINS
ENZYME
--
in troductionto proteins
functions immnnoalobnlín
G
-
act astoxin, antibiotics andvatines 1500
amino
acidslong
protein stuncture
VanderWaals
Atom
with
representation
Surtale
represent
colouys
Surface
and
pydtein
=
representation
of : looamino
thesurface
Show alid
biQ protein
lysozÿme
diagram ribbon or
cavtoon
secondavy showthestynctnye proter of
henices
alpha
beta sheets
nighly
internution
resrstance
thermaistable,
withneighboring
todenaturation
torstability require
styands
-
mod
el spacetilling
atoms
them
,fimthespacebetween
representsmolecmie a
0freiative
byShowing sizes n
ball -and- Stick model
ntoms
connected
by stiuksshow
bonds atoms
andangiesbetween
aminoacids / STA
amine carboxyl
chainRsíde
backbone
peptide
primary N
amine cayboxylicaüid
'COOT
-
H alphacarbon
( chiralcenter)
number =
A1foursitesare bydifferent
occupied
20chival ( ne
centers)
amino
groups
number
aud
ofform
is Asymmetyic.
S+ereoisomers
, ,
formpolypeptides peptide
bymaking bond
as
reaction, prodncesH2d
by -product Condensation
peptide
c Hz R -H:0
R 0 bond R
Il
NH: coo * NHS- c COD NH31- N C CD0
H H H H H
peptide bond
covaient >strongesttupeof moieuniar
bond bond
chavacter
partialdouble
bondnas
rigid as
it A
..
...•-
0...0.
cis
H
trans isomerisation
0-
H
==
C- N bond 1.32 A
normalC-Nbond I-4QA
bond CEN 1.27A
1enqthshorter
more
viqia
bond
Z
H
TYAnS Cis
stable more ©olivia_liying
,aminoacid
U
chivality
mirvor image
#412/092CA0/1V
molecule
D- (somer and L-isomer
identify nsingCORN
is non
rmie
COoH
doJ H
on -
its achiral
Superimposable
COOH
H
left to right to
NH2 R NHZ
--
Levorotary L
steredisomer DextrorotatoryDStereoisomer
nre
abletotwisttheangieofpolarisedlight
steredisomers
right, L isomer turnsporarisedlight to D
toleft isomer
isomeris a nature seletted asummetricisomer
in mammAls
L
only arefoundin proteins
Lisomer
thalidomide
Rlrignt) thalidomide
babyNON.Te
was
for
prescribed
fof scieft) thalidomide
nansea
duringpregnanty
in
preventlimbdevelopment
teratogenic,induce birthdetects
D-serine
systemand
azwitterion
forms
íonsaISoknown
are
D-asparate
ataspeciticpHknown
asdipolar
mn
found
asrsoelectril
nervous
centval systemand
poínt pI
endoerine
,
chargehave
nentralnet NUNR
amino
aud
buffers aroup
carboxyi acts
and duetothepresence
ofamino
H3N COSH H3N COD H2N C0D
qlyciniumcation glycine Zwitterion alucinateanion
PH pI pH PL PHZPI
nentrainetcharge
=
alidic bAsil
H H
O
H* 2 =
Lnal bufferina N-H
•
regions
H*
H 0H
primary amine carboxylic audcarboxylate
©olivia_liying
, -
nonpolar
H3N*=
C Coo
H
- C
CHJ CH
CH3CHS
C
CH2 HaC CH
SH CH2
H
HaN-C --coO
cHa
-
Alanine Valine Cysteine Proline Phenylalanine
Gyeine A P FHM
.••.
core
pydtein +buried(nside
C 0- C amino
non-polar acids011
avehudrophobic
H3 C CH CH2 CH2 inclndes
cysteineand
tryptophan
-É
0-5-5
CH2 CHa
1Argest tryptophan
CH3CH3 CH3
D- : glycine
smailest
CH3
Lencine Isolencine NVANmethionine Tryptophan
Itigdedd M W
polay
0-0- 8-0- 2-=1
CHa
OH OH CH3
OH NHZ0
NHZ O
Serine Threonine TyrosineAsparagine Gintamine
S N Q
t charge(basic) chargel acidic)
charged
amines C
NH 0
CH2
AHT
Histidine C
Pua
CN
S-E_É_A
MNA 04°
0 0
1
NHgt C=-NHS
NHZ
Lysine Ar qinine©olivia_liying Aud
Glutamic
AsparticAuid
K R D E
, Glucine
its sidechainsmall(H) ASiS flexible yotataole peptidebond are
nenrotransmitter
forms by Rgromp
%restrilted lextept glytine)
andhasnoD ¡Somer
qroups carbon)notan
avound 3
opticalisomer-(onm
Cysteines
athiolqvoup
has
cantoother
bond + toform
custeine bond
bydisuiphide
cystine
a+2H 20-
HOOCCHCH2S-SCH2CHCOOH
cystime work
outside to
of theproteinsthathave
>oxrdation intreasecen
nse to
disulphide bond
NHa drsuiphide NH2 losee- Stability
-- -
bond insulin
0 pepsin
proteinsmetals to (h
binds phospholipase venom
dee
NH3* NH3° Znit
Coo C CH2 SH *t coo~- C CH2
NHqlt
H H
more easily likelosthydroxyl(-0H). H1S
Histidine
basic
1owpH +Chorge
hign pH: nentyal
acceptsHtbelow
nentralpH
Side tophysiological
pKaClose PH duetoits chain,imidazole
ring, histidmnea(1.4)
has
can
existinbothnentraland posrtive
charge
-
to PHchanges,switch
auditysensitive
surrounding stateaccordingto
-
Strongly
metalsbindsto
n0tin human
charged
Zn>t H1 H
CH2 C CDOH
NHz.
poly histidine
ta0isnsefmi
forproteinpuvification
precursor
for histamine SNINOSINT
converSion tohistamine
histidine
AromaticAminDacids
byhistidme
decarboxylase
absorb
lignt
diet essentialin human
phenulketonuia phenyimanine
hydrbxylase
excess
down inability tobreak phenylaianine Atyrosine
phenylalahine
treatment
10W
Phediet theproduction
tyrosineis needed
for
avoidsaspartameavtifruial
sweeteners of nenvotransmitters
aspartit auid phenyialanine untreated
PKuleadto intenetnal
disability
©olivia_liying
