Bond made peptide bond

499
"
Monomer : Amino Acid are varied and interact to :

form Various bonds ↳ condensation reaction

carbonyl acid r

:i:ns"ic
Aminocname,
Basic structure :
group group enamel
⑧
:
"

in
'
in
÷÷÷:÷ :c
.

beaus
once this forms 2 amino acids dipeptide
fgfdeprdoi.la?n9isYendmufe [ 3
:
,

hydrogen atom

or more :
polypeptide
weak
Level of protein structure

pµfTf
:

Bonding
a

|
" stages ) involved :

Primary structure
✓
a. a joined tgt -

polymerisation ① Hydrogen bond -

weak

Sequence of A. A resulting in polypeptide

-

!;jn fat:!dwj:b
-

snuowiimrminedbmm.i.io
""

secondary ji;
. -

formed by weak
② " ni ,
formregular shape has become denatured

ynothandwriting
protein
-

my
hydrogen bond
,

d helix or 13 pleated increase kinetic energy unfold

.
-

twisted I coiled
③ Disulfide ( covalent ) bond
Tertiary structure - maintained by :

bonds ( numerous weak) formed between 2 cytosine a. a

hydrogen
-

( very bonds )
strong strong
,

-
fold into 3D shape -

ionic bond
-

disulphide bridges (strong ) these bonds are sensitive to : temp

Quarter nary structure
multiple polypeptide chains
↳ can break
pH

one or more polypeptide Main Examples Of protein

linked in various ways
↳
-
-

chain joining tgt . -

prosthetic group ( nonprotein )
① Haemoglobin ② Collagen 1%8 DENATURED
A 3D shape is important but sequence of a. a
determines it first
 GLOBULAR FIBROUS
[ metabolic ]
a
-

.su?!himgegYtifoendioinedY
> structural '

:& infamy.bg?9n9sainhnaaes
fyoundin
-

each chain arranged tendons

around Eg collagen
haemggnvp Shape lrfvnotionof
:

rPROTEINO-itaonmiin.net#i osewomanan
contains iron MOI .
lo :
unbranched polypeptide
that can bind

fa
: .mn
"
.

Gii nm itesi rosin.ve/:.m!q:en!:me:is

.
30 chain twisted into second
:

eatra :
helin

TEST FOR PROTEIN 40 :3 of the chains wound tot

in a way that fibres are
Bivret test
-
-
detects peptide bonds wound into a rope

:
:{Igniting.ie?n::snii neita-
staggered ( spread )
ends
-

provides strength