I Hin I 1
H20
synthesis of peptides: a b
C - N Y +
C r -
-
C
-
-
C
H 1 H - H
I 1
I it I
levels of protein Structure :
Primary Structure Sequence of amino acids influences how the
ypol peptide folds
:
Secondary structure :
O,H and N interactions :
form hydrogen bonds -> Alpha helix or Beta pleated sheet
Tertiary Structure Folding of :
a protein into its final shape due to R
group interactions
Hydrophobic and hydrophilic interactions bonds
-
·
lonic
Hydrogen bonds Disulfide bonds
- -
Quaternary structure Tertiary interactions :
between different subunits
Globular proteins Compact Spherical proteins formed
water Soluble , by hydrophobic interactions
:
,
↳ ie insulin .
Conjugated proteins Globular proteins with prosthetic (non-protein) component sie Haem in
haemoglobin
:
a .
⑧
Haemoglobin :
Quaternary globular conjugated protein with two a and two B subunits
↳ iron 2+ binds with
reversibly Oxygen
·
Catalase :
Quaternary protein with 4 haem
prosthetic groups -> breaks down
hydrogen peroxide
Fibrous Proteins :
long insoluble molecules formed from small repetitive hydrophobic, ,
amino acids
·
Keratin :
fibrous protein in hair skin and nails
,
Contains large proportion of the
sulfur-containing amino acid Cysteine
·
a
many strong disulfide bonds
·
↳
Strong , inflexible ,
insoluble
·
Elastin :
Fibrous protein in elastic fibers ->
walls of blood vessels
Quaternary formed from many tropoelastin
·
protein molecules
↳ Allow
expansion and recoil .
Collagen Fibrous protein Shin , tendons
ligaments
·
in connective tissues
:
- ,
·
Three polypeptides wound together forming a rope -> hydrogen bonding
↳ flexible
long strong , ,
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