BIOMOLECUL.

li# * How to
analyse the

cell fractionation
chemical
composition of
( Mortara pestle )
a cell
?
living
↳ Trichloromethane 'd
tissue 1) pestle
→

filter
( cclzcootl ) Mortar
nags

÷
insoluble ]
Acid
soluble [ osgauicsubslanes
fraction fraction Biomauomotcculee
Jg
t
,
I

[ Monomers Polymeric substances

}
☒ Amino acids Protein
to monosaccharide →- due to high
800Pa
" " """des -

polysaccharide molecular
→ Nucleic acid
( Mamma , weight

]
and size

lipids →
due to
insolubility

[
Dalton to
low molecular
Biomeiromoleuek weight
are biome 'ao molecules .
?⃝
Inorganic analysis
weigh a small amount of living tissue
( leaf /
1 ✓ live.de)
it ) called
Dry 1
Dry wt
weight is

4 WET
weight
All water
evaporates
↳
Tissue
2
fully burnt

Carbon
compounds are
fully oxidised to
CO2 H2O
,

↳ rap
-

' '
A removed
Ash remains
to
elements
inorganic
contains
elemental
& can be
analysed by analysis
 5

2
I
I 1) 0)C)Ca#

0711J
3
"
1) G) C)
=

)
" "

6 ,

7-

:
 AMINO ACIDS →
substituted methane
Amino acids

CHY -

methane
H=R
µ
Protein Non
d
"÷%÷d
-

H
µ - -

Amino protein
I acid
, amino
H Amino
( ao )
acids

Variable
R=
group
I Amino Acid
-

( Simplest Amino Acid

)
H
Glycine
-

Ctlz Alanine
4113 4h04
-

COOH
Serine HI
HII 4- coots
g-
-

ctegotl
-

Tel H H

cagey cysteine
-

Alanine Serine
Thiol
442511
HI 4- COOH
-

cysteine
 442 442
S H H s
4112 STS ctlz
- -
- -
- -

/
1
C- COOH C- COOH >
HI HN
HII
4- WOH
- -

text won
-

<
-

"
,

"
" ti
cysteine cysteine Disulphide
bond

Note →
Glycine
-
CYSTINE
Amino acid
*
simplest ( Dinner
of cysteine)
*
Inhibitory neurotransmitter
inactive
*
Optically
A A
H
l
E- É*B
l
C B C- COOH
E
HI
-
- -

al
Tt H
D A

Asymmetric
carbon symmetric or
carbon

or Achiral carbon
chiral
carbon
→ show optical activity
¥

Iggy
n

Nicol 2>9
prism, o
solution
1 ,
☒
I
i.
optically
active
% i -
→

plane
⇐

polarised Right left

light L
rotation Rotation
j
d

*
Peptide bond
formation optical
rotation .

41131,0 HSH
,€ 1,0 41131,0
1¥
H - -

C- C- OH H -
N -

C- c- OH H -
N -

C- c- OH

it -

it 1
+
in 1
µ
-

(CONH )-
1.

a- ¥?! ,¥É§ N -
93,0
C- C- OH
Ñ I
reptile µ i
peptide µ i
µ H bond H
Left N-terminal
bond
Right
end
NÉE C-terminal end
 CLassficahouofAminoaudf-Protee.ir
Amino acids

Non-protein
(
Amino Ornithine
teds ?Y
1) On the basis
of Nutritional retirement Taurine
in

obtained t× synthesised
⑤ essential Artsybody
-
Essential Any
from -

diet Dispensable
or
-1-3 Ads Arts
/
.

p
phenylalanine Hydroxylation of
Tyrosine
-

>
( )
>
precursor
v -

Valine om

T Threonine
*
Thyroxine
↳
-

Dopamine
Tryptophan
*
> serotonin & Melatonin
precursor of
-

Adrenaline
I -

Jsioleecine 15 Hydroxy
-

tryptamine
*

or
M Methionine Epinephrine
-

histamine

{
H Histidine precursor of
]
Basic
-
adrenaline
-

Nor
present in histone proteins
*

Arginine
-

DNA
A +
amino or
-

( Bashi) (Audio)
aids L Lysine Nor
epinephrine
-
-
-
-

Leucine
Off Melanin
L -

(protein )
d
Histone skin
pigment
Melatonin
trormone

of pineal gland
in brain

/ ornithine
cycle
urea
cycle
indliner
-
Non
protein Aot .
-

cells .
 inside chain
Have -

Ntlgngmoups .

2) Chemical Basis :-/ ( R)

at .Au- AAG b) B 4Neeilr# Aliphatic side chain -

COOH

A- → Acidic B- Basic G-
Glycine
)
/ nonessential carboxyl
Aspartic acid A-
Arginine
A- Alanine cmon essential
group
-

A-
-

Have

Glutamic1
F- tuine Valine
v
G-
-

more acid L
OH
Lysine
-

Leucine
- -

cool I
isoleucine
qrpsin É
-

'd
sidechafephu-m.ae MHz
-
-

[ asparagine
amides
[ Amide ]
v.

Glutamine }
Non-essential

era ST

d)
5¥
.ge f.) AA ⑤
912min00
acid
proline
serine nonessential PTZ
←
Cysteine d
-

non-essential
essnumeial Methionine Threonine p→ Phenylalanine
7-
Tryptophan
Tyrosine
non
T
-

essential
-

MHz
Ammonia
-

MHz
Amine
|-
Imine
Iminoau 'd
 Charged but
electrically
neutral
R ✓ R R
H¥iÑ d- ⑦ I
cooÉ HA coin
H§☒ g-
coat -
I c-
-

- -

- \
1 I
Ht
(
>
H H H

Hybrid __ Zwittee Anion

+
"
Calton Lion
exists at pH ( High pH)
( lowpte) known as Isoelectric
point >

GAS
Neutral

O -

c-
c - -

Imine Acidic
- -
Basic
-

- o
0
0
- -

① Amide

- -

- -

Basic

① Amide 0
✓

O
- -

-
-

Audit
[ o
 Hetero Amino acids
PROTEINS *
polymer of
① PRIMARY STRUCTURE
A- Az AA
linear
AA , -
-

AAN N C
}
- -
- - - - - -

T
terminal terminal
peptide
C

② SECONDARY STRUCTURE >

N
g- helix
( Right
' i "

, )
handed
H-b°①
,
I 1
I i
keratin
,
egg
-

1
1 i l
t

13 pleated
,
'
, I
-

sheet in

fgfibroinofsi.lk
mammals
! '
)
keratin
B-
H -

bonds ↳ Birds

③ TERTIARY STRUCTURE
disuephidebonds Hydrophobic

→÷zÉ•ÉB%3z
interactions
↳
mainly responsible -
bonds

for biological activity

of proteins / enzymes) .
s-s-qy.pt -
"

"I

ai
-

:*

Vander Waals forces

i-
←
.

Ionic / Electrostatic interaction .

④ QUATERNARY

yglob%aBzoBB.gs?-3zoBBag-uaem
STRUCTURE

/ -
-
-
-

z-qi.EE:7?sjjsH-....
-

co
-
- -
-
-

B- globin

• •
✗ -

globin
F.
Vander Waals
forces
structure
Quaternary →

formed by interaction between

2 or more
polypeptide chains .
 Ñ- Hetero
polymer handed
of aminohelices
acids
structure only right are ✓
(5)
observed Myoglobin
(
Chain
I
.

n.te-m.nu/peph--debonds
c- terminal

MHz ←
/ N C
muscle
pigment
terminal terminal
free 153 d-As single
. .

polypeptide
Fibroin

*
keratin threads

( night
helix
( p pleated
-

sheet) 3zqBBBg

p-glo← → ✗ -

globulin
•
•

Fetz (Ferrous )
-
•

globin ( Anychain)
146
p
- -

essential
I
,
/ -
14°)
Adult Hb)
for biological gap , (
activity of proteins 4- globin
d t
✗ay ( fetal Hb )
enzymes /
141 AA chain ,
C N

H -
bonds

( }
o

* .
 -
¢43 ) -
aliphatic
side
chain
(
Hydrophobic )
¥iÉ°M MHz
,
AA

{ }
He •
-

t.ir

↳
or

electrostatic
attraction

81
✓

.
C