Protein Structure and Function - Biochemistry

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↳i
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O ⑧ It O H
Il Il
C



% hi
Re
C
·
H b
H

Ba


formed
DEPrideBords Condensaon/dEHyDRATON Hydroxyl from Acid's
CARBoxylic Acid And
Hydrages
REACTION in Whic The one Amino
group
: Via a



FROM Acids peptide Bord
REsuring
ANOTHER AMONO & Amino ARE Lost As HO in a
Group


ionvzaron in a polypeptide : When an Amino Acid is FREE (Not BoodEd To Another Amino Acid)




It It
R
its AminE is ourtaBLE and so ISOME Amino Acids Are An TONABLE
group
is MS &
Carboxyl
group
a .




COOT
iOnrtABLE side CHAN Too) However when a n Amino Acid is Bod The Amino &
Carboxyl AllC
↓
.
, ,

coo-
Hsts -
Departe Bord are HIN
1
the

groups participating
in n o t iometable .




, immizable IONABLE


peptide influences
Body
This is not The has ionreason , as
only way the



Distance Between increases The FREE Acid Bonded Amino Acids
charges
The
Carboxyl likely To iomert, Amino
group
,
C is LESS



FURTHER AWAY From
MEGAINE CHARGE
BECAUSE WILL BE MORE ATTRACTED WHEN M IS The
PROTONS TOMS




PKa
postNEly
charged
Amino INCREASES In COMRAST THE Amino MORE
Likely To
group
is

grap
. .
,




Loweringrspka
LOSE Ms
PROTOw ,
.




DIHEDRAL ANOD THE
ANGLES
: THE BETWEEN THE A CARBON LAMINE OR THE
S CARBOXYL
ANGLES
ETHER

GROUP Group
.




& AminE L
Carboxyl
ThEY are important Because
They Tell
us About The Secondary Structure of The protei .




Pkz PK ,
HELICES TENd TAKE of DIHEdrAl WHE BSHEETS TAKE On ANOTHERSEY of Dihedral
ANGLES
& To On ONE SET



DECREASES INCREASES of
Angles THEY ARE Because Reduces
ANGLES
ARE WHAT That Combinatron

Angles
THE
.

particular

hrderance. Dihedral
displayed ramachentran plos
angles
Steric are un a .




Bowling -
If
Secondary
#
us WHAT STABMES Structures ① N- Ca
Hisg
.
P LE :

#
of THE Y C


Psitng
Bonds w/
%
Ca-C
Grog
in < HELICES , THE
Hy En AME LE =



PH
↑ N
Coo-

THE CARBOTYL Acids
I Ammo
Away
OXYGEN
.




STRUCTURE I Y

-
~
1000 ~
-
600
& HELN




1200 1200
B SHEET ~ -
~ -