proxin.

signaing
pnojnp pron nece
a. oh
membAne ces compon@nt
o s tia esse ne They
PROTErNS OF
FONCTIO
S
celus moSt 0fofmass dny op
507.
ins.Sr5! She
nmonolecoles
2) Vt Motens
e
Solpus. -
elemenismay Adoitioa
Nitr0gen -
Orygen -
Jr Haydnoge
organie
molecUlES Pnottlos
e
made PRoTFIN
of. p
Somehomones he DnotelnS

-insolo.

The oxygen cannyi ng p'gmets haemoglosin and

myoglobin e potelns

Antilbodies ohie tok and desthoy invading mIchoOnoa

nisms ane pmoteins

CoLLSgen is another paotei n add 1hat adds sthength

to many animel t1ss0es suh as bone ánd wls

Haia, nails snd the sunfa ce layena of skln onteins the

p0tein kerSo.

Actin and muAsinehe he photein nesponsi bie

muses.

Poteios be
food stonae pOdu ts
may
CA sein in milhO

ArmiNO ACIDS
Pnottins e moe up op ot o Snalle mono neS CA
(inke oqesne:
hese

The sming cids

joined by peptide bords
 Amino cds Ahe
Called polypeptidesSend \9l0%2,
are led dipe pthóe.
d m o cids.
Thee ane 20 dipenen

(cooH) hicn is tatehedh

cAnboy ghoop
eahbon to

The R g20up (Remsidual ghouplside chaio) s -Ihe

Changes beeen hem.

The qene hal ponmula pon amio Jelds is NHo- RCH- OOH.
Rgroup

Anine

(meoRTANOE oF THE R-aRoup

The Q-ah0op detn nies he active site on an enzyne.

t acts ike necepto On ne eel membAne

It de te mines the bondig between othen mino c ds.

 CHAAACTERSTICS oF miNO AciDs
R-gnup wnich is
some wil nave no -polah
gop
) Anino aeids
e So Loble in
uwstea s 1ne ine On

t) They e Small nd hence an pass

men bnne. 1hoogh1ne ceu
i)The can be eystaized.

)Amino a ds e
ampnotenic.
NH is bTsic.

Coo is scidic.

The cnenqe of an 9mla0 ACIo s p based on 1he nediuin

shicn it is placed io.

This is becoU)e he medivn in which he dnino dcio is

placedin deteanmines th2 wey in wich the NH ond

COOH 9ouPs ionize.

NEUTR AL MEOIUm
The smiio cid is lonized in nevtal mediUn.

(4haS Zeo
chenge t-e neuthal amino cid.

ThepR of the ytoplasm is neutNal hence mino deds io

he cybplasm beome ionized ie NS snd oQ.

 S0eUtNO
9lalne
aninoCO
he
he.anino cid
whiah
Tne pH vatUe in
s 1he iso elec9ie point op

i becones pOsi1NE.
he s nino

BAsIC mEDIm
The anno lcið becones 0Egative

H.

FoRmAnon OF PEPiDE OAS

H conde nSation
H

hydroly
Peptide

the
The OH om
Dmine q00p bond to fon m wteh moecole and (eAve
Bne peptiOe bo.
 P(osle
STRUCTURE 0F PpOTENS
The protein shoctnes consist op:rot
primeny'
-se condy
-ttotieny
-qantinay

PRImAQ sTRUCTORE
Thes e ehe sequences op amino aeldS joined rogethen
by peptide bonds cha'iS.

.p one smino ecd is ltehed ne phoren energes

The pnlmay apected by

incneaSe io denpeaae berase pepti Òe bonddon+
bneak d e to t h i o

The lengtn o the phoeln e mains the sYme even

apeaneeting:
SEONDART STRUCTO RE
The polypeptide cnan coesnt nemi plat and sthiqht.

They opten col into 9 0n k s k e shape catied heLX.

lydnoqen bonds fonm behoeeo tie dmio is.

chhe.
p1hey coil op 4hey fom oC heix stnu

-kerala which is ound i nails, haine+c.

 oi ling snd
Hyonogen bonós ne impontant in onden to pomm
bonding benseen tne polypeptiÛe
potypeptdÇ chain.

W)HYDROPHO BIe (N TERncTION HO2o PHNLLK, (TERACTION

hen hyo nopholeic q0ups ane ctose togenen in phokins hey
4eno to elump togetne poming a qlobukm shope.

ohen hydrophgue qhoups Ane lASP ogehen they tend

posh eechothen out slde thass chagìg the shape ap paoeto.

TERTIARN STRUCTURE
fotding op the poly pephoe chalnis mohe comple.

Ech ype of prottin has its oun panH culA snd uaiqve
te
tiary thucone shis is e7uci a\toi s
uncton.
The potypeptde polos ponming au etaòsop complex 3D
sha per
These shapes ane help in place Hh t di freent
ehemi Cal bodsj.e ypes
bonos and
hyónoqen bonos,diSulpide bonds,ionic
hydnophobic ltehetton:
QUATENARY STRUCTURE
This iS
qlobula stnuctone nai conSists op
mone 1nan Oe
polypephde enaln ajpined ay hynen.ionie dsonióe
ed
baidqes and hynophobie and
hyonophyuie integotions.
haenoqo bin 'is maoe up op
t
C hainspolypeptióe ehalo oined
bu these bondS i-e 2
b chains
with + oning ids s
wi1h46 amino Ssds.
QLOBULAR PR0TEINS
These ane proteins nich ae sphenicala nd o mpact

They ean cunl up into a bal shape and heve hydnopholaic

and hydtophy ic inenactlans.

|They Ahe mAdo op of many poype ptioe cnai ns nich ehe

Op so thnet hydnophyllic pants ane ootusa nos neseAS
4he hydophobie pahts face' tnonds

ThiS makes 4he pA0tein soluble io oate% Ad ahe +hons

ponted in pluid.

-Antiodies.
-hohnones.

many qlobulah phoelos hYe thei nole in metsbolliC

neNtions.

)
HAE M0GLORIN
|Hs dn ygen cannying Pgmem pound in RBCs

made e op 4 polypeptioe châins 1heneroae it, has a

quatenay Sthochse.

Esch chein is photein known as globin.

Haemoa<olin consists of 2 4yps of globin moleeuies

- 2 0C qobin
molecules (2 potypeptide cnaing).
-2p ylobin moiecules (2 potypeptide chains).
 COnditions Such as sickle cetl An aeiid Aloslnn
heplaced in he chain i.e instead op tha
30TOmic eci ,wnlch is polA, 1heae iS Vaien, which ig

Prostnetic qroups ane

a poeins consisting of amino sids
e

-n
gly copsoteins the prosthetic ghoup )Sipids.
-ln haemoglokin he prosthetic gnoup is iho.

FBROUS PROTENS
These ane mede op op long insoloble polypepide chns

that ahe tightly aoiled AhoUnd ech othe to fohm

Aope shepe.

The chains ane held togetnes by many bondSwhich môre photin

sthong eg.
- disolpide.
-hydhogn.

Due o thes sthengthe hey'ae usoSuy found in 1he

suppontive

kenatin osms hai,nails.

cotleg en s fhe suppo9tive tissve pound in comtillage and
teeth
 3STRUCTURAL DIFFERENCES5obon o3o'ciel s

CoLLA GEN INSULIN

ucto )EibnouS pOttin. JaSieal Gobu la paotein.

tas di sulpun bal dges and

Only hy dnoqen bonds
to.004hydrogen
Have poly peptide chains
cheins
) Have 3 polypeptide

nepeoted sequence op
of
Have no nepesed sequen Ce
i Heve op amino scids
Jmio ids

Flave 5|&mino
cids.
mo%e thdo (oo
(O0
Hae