Answers :

H Essential and Non Essential -

AA :

Essential Amino ace 'd -

Their carbon skeleton can not be

synthesized by human
beings .

Histidine leucine Threonine

Arginine Isoleucine
°

, ,
, , ,

lysine Methionine Phenylalanine Tryptophan

, , ,

and Valine
I Any Help In Learning
8 in number These Molecules Proves

True ly Valuable ]
Non essential
- =
to in number
•
Their carbon skeleton can be
synthesized in body .

Glycine , Alanine , serine .

Cysteine Asparagine ,

Glutamine Glutamic Acid

.
Aspartic Acid , ,

Proline
Tyrosine .
.

② General R kn 7 AA :

③ structure 9 Proteins :

( as
Primary tune :

Denotes the number and A As in proteins

sequence g
•
.

Maintained
by Peptide linkages
•

If seq .
in
changed the peptide ,
in also
different .
charactershis g Peptide Bond :

Partial oouble bond

o

•
c -
N bond in trans in nature and thus no
freedom g
rotation due to double bond
partial .

°
The distance in t 32 -
Ao
• The
angle g Rotation known Ramachandran Angles as

determines the
spatial arrangement / orientation g Peptide chain
.

Numbering g AA in
Proteins :

On the
left side there will be
free alpha
°

one amino
group
this end is Amino terminal ( N - terminal ) end .

and this is also called the first AA .

The other end chain in

Carboxy terminal end (C terminal )
°

g
-

and this in the last AA .

Primary structure determines

*
Biological Activity .

(b,
secondary structure 7 Protein :

ci , H bond
°
Preserved
by Non covalent forces or bonds like ciii Electrostatic bonds
( iiis
Hydrophobic Interaction
Vander Waals
Usually in ③ forms is
force
Most stable and conformation
cis Alp hehe line : common
g poly pepkglehain
Spiral structure stabilized
.

by Hydrogen bonds
°

;
between
NH and C O
groups
-
- .

handed
Generally Right
°
-

.
Proline and
hydroxy proline will not allow formation g a -
helin .

.
As in
Myosin . Actin . Myoglobin .

dis p Pleated
-

sheet :

Almost
fully extended
°

stabilised
by H bond btw NH
& C o
group
- -
. .

Proteins like Silk fibroin

Major structural motif Flay,¥
o
in
.

carbonic
and anhydrase .

•
In terchain disulfide bridges stabilize these bends .

( iiis Collagens helin : Triple helical structure in

Collagen .
 structure
(c)
Tertiary :

denotes structure whole

protein interaction
3D
Hydrophobic
o

g
Maintained coral lent bond such [
.

by Non -
as -

Electrostatic bonds

Tertiary structure
by protein
native no stable
! -
Vander Waals forces .

structure
°
Most
enzymes
and
biological active proteins are in
Tertiary .

Ids
Quaternary shucker :

certain
polypeptides aggregate to
form functional protein
o
one .

°
Protein loses it
properly if subunits are dissociated .

forces T H bond
May be chain Monomer
-

• . I -

Electrostatic bond
-

2 chain Dimer
L
-

Hydrophobic 4 chain Tetramer

der Waals force
-

L Van .

•
As ca ) H b : 2x & 213 chains .

( Heterodimer )
( bi Immuno
globin : 2
heavy & 2
light
( c '
Cma line kinase : Dimer
Id ) L DH : Tetramer .

④
Coning atedPI.es :

combinations
They protein with Non
protein ( prosthetic
•
are
g a -

group )
•
Classified as
follows :

i is
Glycoproteins - Protein +
Carbohydrates
•

hydroxy group g serine or threonine and a wide

group
and
asparagine
of glutamine form linkage with
carbohydrate
As and Proteins
group Antigens
=
Blood serum
many
When
carbohydrate 9 9 and called
by viscosity they
* 10% a
are

as
Mucoprotein / Proteoglycans .

Iiis Lipoproteins , Protein + Lipid

.
Present in Blood and on cell membranes .

ciiis Nucleoprotein : Protein + Nucleic Acid

As - Histones ; DNA contains -

re
charges which combines with
+ ve
changed proteins .

( in Chromo
proteins : Protein t Coloured
prosthetic group .

As - H b Heme ,
Red 5 Flavoprotein ( Riboflavin Yellow)
→
,
 Visual Purple ( Vit A. Purple )
→

(VI Phosphoproteins : Protein + Phosphorous .

vitellin (
As - Casein ( milk ) &
Egg Yolk )

(Vil Metallo proteins : Protein + Metal ions .

As - Hb
( Iron ) , cytochrome ( Fe ) Tyrosinase ( Ca) .

carbonic Anhydrase ( zn )

⑤ Classification g Enzymes :

3rd
•

By IUBMB
system : 1st
digit = Class
digit = Sub -
sub class or
,

2nd
digit = Sub class-

4th
digit = No g
subgroup
in
enzyme
.

o 6 major classes : list .

( as Oxidoreductase : Oxidation g one substrate while reduction

g
other .

As Ah t B A t Bhz
: →
z

Alcohol 1- MAD
+
→ Aldehyde + NA Dh tht
( Alcohol
dehydrogenase)
( bi
Transferases Transfer substrate to
group from
:
one one other .

As A -
R t B → At B -
R

Hexose t AT P - Hexose -
G -

phosphate t A DP
( H exo kinase)

(c '
Hydrolases : Can
hydrolyze ester ,
ether , peptide or
glycosidic bag?
by adding water .

As Acetylcholine + H2o - choline + Acetate

( Acetylcholine

digestive
esterase )
* All
enzymes
are
hydrolases .

( di Lyases Remove groups

:
from substrates or break bonds
by
mechanisms other than
hydrolysis .

As -

Fructose 1,6 bisphosphate -

Glyceraldehyde -
3 -

( Aldolase) phosphate
+
dihydroxy acetone
phosphate .

(e) Isomerases : can

produce Optical ,
geometric or
positional isomers

or substrates .

As -
Race mares , Epimerase ,
Ce 's - trans isomerases

Glyceraldehyde phosphate Trios acetone phosphate

-
3 -
-
Dihydroxy
( e phosphate isomerase)
 If '
ligases : link two substrates
together usually .
with the
simultaneous hydrolysis og ATP .

As -

Acetyl -
CoA t coz + ATP -
Malonyl -
CoA t ADP + Pi
( Acetyl-CoA
carboxylase)
⑥ Coenzymes :

*
Holoenzyme / Enzymes Apoenzyme
+
Coenzyme ( prosthetic group )
•

Coenzymes maybe divided into two

groups [ FMN finning FFA on F ADHD
: -

taking part by Oxidoreductases [As NADP NADPH]

'
(a) Those in reaction .
-
-

in reaction other than H

(b) Those
taking part transferring groups
.

As -

coenzyme -
A

salient
features g Coenzyme :

c ' '
Protein
part gives for machine
the enzyme 3D structure ; but the

group
in
transferred from / accepted by coenzyme .

(2)
Coenzyme is needed for biological activity .

(3) It in heat stable

(4)
Coenzyme can be
separated from enzyme by dialysis due to loose
combining
able to convert
large
.

(5) One molecule og coenzyme

is a no subs bat
y
.

( at Most the derivatives Vit B complex

g coenzymes are og .

⑧ Factors
influencing Enzyme Activity :

• Gm short : ca )
Enzyme Concentration
(b) Substrate Concentration
cos Product concentration if , Presence g Activators
(d)
Temp .
(g)
Presence g Inhibitors
Ce ) ch ) Presence og Repressor / Depressor
pH
(
i, Covalent modification .

(a)
Enzyme -
concentration :

Rate of a reaction or
velocity in
directly proportional concentration
to
enzyme
increase
vet will
proportionately with cornet
• .

9
.
.

enzyme
the substrate in unlimited
if .

used in
This
property in
Endpoint Method
•
.
 cbs Effect g
substrate Concentration : As substrate concentration is

increased
incr the
velocity is also in the initial phase
Vma
but the curve
flattens afterwards .
'

The obtained
main
velocity is at IVmax
•

✓man -

km es }
(c) Effect g Comet g Product : As the .

product concentration 9 the reaction slowed .

down .

(d) Temperature reaction

Effect 9 : the
velocity
medium in
g enzyme increases
when ten ata increased ; reaches maximum
per
a
g
re

and then falls ( Bell shaped curve )

- opting
q
•
The temp at which max .
amount a substrata ?
formed / unit time
is
Optimal Temp .

activation Ten
molecules
As
Temp 9
gets
°
→
more

energy
,

and thus collision

probabilities 9 this Rate IT

has
(e)
Effect! pH : Each
enzyme
an
optimum pH ,
on both
sides
og
which the
velocity will be
drastically reduced .

Graph in bell
shaped curve .

Comet g Substrate
•

Optimum pH depends on
Temp ,
.

, presence
, zu
,

.
Usually optimum pH =
6 -
8 .

[Exceptions Pepsin I 2 :
= -

etc

Al Kaline phosphatase =
9 -
lo
]

:÷:÷::c: :÷:÷
IT
⑨ s

::
"
" .

(21 It denotes 50 's molecules are

g enzyme
.

bound with substrate molecules at that

particular substrate concentration .

Concentration
131 Km in
independent Enzyme g
.

41km and characters hi feature

in
signature g the engine in its .

(5) Km de tones the

affinity g enzyme for substrate .

↳ km
I. The affinity An
⑥ Enzyme Inhibition its clinical
&
Significance :

IAI Competitive Inhibition

normal substrate
: Inhibitor molecules are
competing with the

site
molecules
for attaching the active
with

g enzyme
.

Inhibitor will be structural

analog g substrate
°
a .

Competitive Inhibition in
usually reversible without .

Excess substrate abolishes inhibitor

Vm¥
.

,
•

✓man - - - - - - -

•
Km will be increased h inhibitor
I
.

° ✓ man remains same .

1-
As - Succinate
in
dehydrogenasemate
inhibited malo
reaction km
"
New km

by .

(B) Non -

competitive Inhibition :

•
It is irreversible .

.
There is not competition between substrate and Inhibitor .

•
The inhibitor
usually binds to a
different domain g
enzyme
.

An increase in substrate does not relieve this inhibition

generally
.
•

without
will not
change Irma if ur qq.h.in

!
°
Km ; .
→
f

As -

( as
cyanide inhibits cytochrome oxidase .
Irma with
Inhibitor
IV.
fluoride inhibits Eno lase thus
man

( bi T
glycolysis .

Km [s ]

Ia do acetate inhibits
enzymes having
les Sh
group
-
.

(d) ( di
DF P
isopropyl fluoro phosphate) inhibits Acetylcholine
esterase .

(C) Uncompetitive Inhibition :

does not have

any affinity for tofree
Inhibitor
enzyme
.

Inhibitor binds to but not

•
E -
s
complex free enzyme .

In this Vmax I & Km A

p ( Regan engine )
.
, an iso

As - Inhibition g
Placental alkaline phosphatase by Phenylalanine .

Clinical Importance g Inhibition :

Pharmacological Action of many drugs may

be explained by the
principle g Competitive Inhibition .
 Cal
Sulfonamides Antibacterial agent :
.

inhibit the
Sulfa drugs will
being structural analog
• to PABA

the folic acid Bacteria and die

synthesis in
they .

• The
drug in non tonic to
'd
human cells because humans cannot
synthesise folic ace .

methyl folic acid

"
(b) Methotrexate : It wi 4 amino
- -
N .

9 tin structural to
analog folic acid and thus competitively
°
e

inhibit
folate T reductase
enzyme
.

esseuntial for Cell division

DNA synthesis &

Methotrexate is thus anticancer

drug
•
-

to K and act
(c) Di command
structurally similar
: vit can as an

anticoagulant by competitively inhibit the

activity
-

n 't k .

di Iso nicotinic acid

( hydroxide ( IN H ) : Anti tuberculous
drug .

Three tunally similar to pyridoxal .

Into Ks
•
on
Competitive gnhibi lion .

① Allosteric Regulation & its salient features :

substrate and
o Allosteric
enzyme
has one
allosteric site for Modifier
catalytic site
for
Inhibit the activity
one .

f. ( Allosteric Inhibition )
•
The
binding of Regulatory molecule can
I Enhance the
,
activity
g
enzyme
.

.
So Allosteric Activators Positive Modifier . c. Allosteric activation)

Allosteric Inhibitors Modifiers

ivmanf-mgidithg.IT
-
re

most::: :S: Yu
"
tmed.vn
'n
:::
'

← with -
ne

modifier
salient features : -

la , The inhibitor in not a

substrate analog .
→ EST

Reversible ( ex substrate )
( b, It in
partially cus

171 Effect in Maximum when substrate

km 9 (
(Cl
usually ) concentration Km
(d) Vm an A
structure ( As Pyruvate kinase has 4 subunits )
ie , Have
Quaternary
④ Iso :
engines
.

Physically distinct
form g
the same
enzyme activity .

. Can be Homo mul timer ( same subunits ) ; Hetero mul timer

( Different subunits
can be formed in diff .

ways
in
May be
product g different genes → True 9 so enzyme .

As salivary and pancreatic Amylase .

( 219 n certain cases ,

all the
different forms are
present in same

individual .

Ifs Lactate
-

dehydrogenase ( LDN ) has 5 iso

enzyme
.

and all seen in all

prisons
are .

Same locus
gene ( different
alleles)
(3)
of All
ozgmes
.

As -
400 distinct form g Glucose -
G -

phosphate dehydrogenase
Ig
( G PD )
all them on X - chromosome -

141 Molecular
heterogeneity g enzymes may
also be
produced
after the
protein is
synthesized These called
Isoforms
.
are .

As -
Salic Acid in Alkaline phosphatase 9 so
enzymes
.

③ Disaccharides :

oooo

① ② ③
 Sucrose :

Also known Cane

sugar
•
as .

• Contains Glucose + Fructose

Not
Reducing sugar free reducing groups not available
°
a
as are
,
.

will produce and

.
Hydrolysis g sucrose moleculeone
g glucose one

molecule 9 fructose .

• The
products will change the dextro to levorotation .

Enzyme for hydrolysis g Sucrose Sucrase / Invert age

lactose :
Maltese :

present milk residues

glucose
o
in .

.
Two

disaccharide
•
It is
Reducing .
.

linkage
a -
1.4
linkage
.
Yeilds Glucose t Galactose on
hydrolysis .
.
It in
Reducing disaccharide
°

linkage p -

1,4
glycosidic
.
Petal -

shaped crystal is on

Lactose maltose osa zone

forms
.

°
Osa zone .

c) so maltose :

Reducing sugar
units
2
glucose
.
.

linkage a -

glycosidic bond
1.6 .

.
Partial hydrolysis g glycogen starch &
produces iso maltose .

④ Polysaccharides :
④ Maco
polysaccharides :

•
Also known as Glycosaminoglycans ( a AG )
hetero polysaccharide
g t in Uranic
containing Acid
•
a
, & Amino

( except keratin sulphate sugars

Doestnot contain Uremic Acid )
( Galactose + N -

acetylglucosamine )
gt the most
imp polysaccharide
• in Hetero in Human
group g
.
.

attached
.

Sf to
protein Proteoglycans .

Special ability to hold water thus

producing gel like
mahin

so it in basis g body ground substance .

Structure g Gita
long Unbranched hetero
polysaccharide chain
:-[
°

.
,

Acid Amino
sugar sugar Fn
- -

The acidic Uranic acid (except Ks )

sugar
•

Amino sugar
D
glucosamine or D
gal aches amine
-
° -

•
GAGS have a
strong
-
re
charge
classification c is
Hyaluronic Acid :

Acid Unbranched chain

I ' '
Hyaluronic [ may
.

(2) Chondroitin sulphate . Present in connective tissues ,

(3) Keratin S Tendons ,

synovial fluid &

Vi tenons humor -

(9) Heparin °
It serves as lubricant in
(5)
Heparin S
Joints .

(6) Derma tan S (B t -

3 -

linkage :[ N Acetyl Gluwmsnna;

•
-

+
B -
I -
4 , glucuronic
Ace 'd I
• Lack sulphate group
to
• Non -

covalently attachedProtein .
(2) Chondroitin sulphate :

Most abundant
•
GAG in
body .

Found in Ground substances , Connective tissue ,

widely
distributed bone tendon skin
in
cartilage . , .
cornea & .

Lineage :
[B - I -
4 Glucuronic Acid t
p - i - 3 N
Acetyl g.alga :b?
j

131 Keratin sulphate :

Most unusual
of all hags
•

Doesn't contain Acid ( No Acid )

sugar
•
uranic
any
•
Found in Cornea a Tendons
•

Sulphate content in variable

. Most
heterogenous GAG .

linkage :-[Galactose N
acetylglucosamine F
•
t -

( B -

linkage )

( 41 Hepazin :

It is
Anticoagulant
•
an

and
Present in liver
henge Spleen monocytes
•

, ,

•
Chemical
Preparation g heparin cis
from lung tissue 7 animals .

°
Acidic in Nature

sulphate d idunonic Acid

•

linkage :-[ -
a t -
a L -

F
T
90% in
fully formed Heparin .

as
Heparin sulphate
,
:

o
present in Basement membrane ,
cell surface .

Determines
charge ! Selectiveness Glomerular
filtration
°

y
•

As cell
surface : Acts as
receptors , Mediatory cell
growth .

In cell -
cell communication .
 Found in
cartilage cornea g eye
•

. Occurs as
Proteoglycan ( core protein t H s )

linkage :-[ Glucosamine + Uranic Acid

A
F
( Glucuronic Acid / I duronic Acid )

(6) Per meta n sulphate :

Hide distributed Animal tissue

ly
.
in

°
Found in skin ,
blood vends and heart valves

linkage :-[ L i damned Ace 'd N

Acetyl gala che mine
f
°
- t -
sa

linkage )
l
(B 3
- -

④ Classification g lipids + Short Hole on

lipid o

. Based on chemical nature -

ca '
simple lipid -
Esters g
Fatty acid + Glycerol / higher
alcohols .

(
bi
Compound lipid -

Fatty acid
esterified with alcohol
but addition contain other
in
they groups
.

'd
Phospholipids containing Phosphoric
cis -
ace

Liii Non
phosphorylated lipids
-

cos Derived Lipids Compounds derived from lipids

- or

acid steroids
precursors g lipids As fatty
.
. -

(
d,
lipids complexed to other
compounds .

Function g lipids
storage form of energy ( )
in T Aa

( 21 Structural
component g bio membranes
Metabolic
(3)
Regulators
141 Act as
surfactants , detergents &
Emulsifier
 (5) Act as Electric Insulators in life anons

161 Provides insulation

against changes in external temperature .

( 71 Give
shape & Contour to
body
cos Protects internal
organs providing cushioning effect
by soluble a .

( ai Helps in absorb tiny fat Vit ( AID . Eek )

taste and
ios
Improve palatability g food .

Clinical
in Excess in
fat -
s

obesity
→ Risk
factor for Heart diseases .

cholesterol
( as Abnormality 7
&
lipoprotein metabolism leads to

Art hero sclerosis and Cardiovascular diseases .

diabetes mellitus metabolism g and

(3) In ,
the
!
FA
lipoproteins
deranged leading to
ketosis
are
,

Iodine No -

It wi
defined as the no
g y
Iodine taken
grams
.

up by too
grams y
fat
.

index lunation and

o
9 t in an
g
the
degree og uns a

unsaturated FA
Gt is
directly proportional to content g .

. go dine No I → Uma her a lion

degree A
Butler 28
Sunflower oil 13=0
=
o = .

④ Terms Aquas ondes

: : A
lipid bilayer form
will
-

on

itself under
appropriate condition to
form liposomes

÷ i÷ ÷ ÷ ÷ ÷ ÷
.

← ÷
0000000 Uni laminar
/ Multi laminar liposomes may be formed
.
- .

l.
-
- O

mines
i 0
a. non . . ÷
.
i.
same .

be
,

Drugs Proteins etc

encapsulated
ooo -

enzymes
.

\ -
. , ,
genes may
.

g act carrier to other

( Liposomes by the
liposomes which can as

liposomes have
important applications in organs
.

Cancer chemotherapy ,
antimicrobial
therapy .
gene
⇐Ines , therapy ,
vaccines and di
agonistic .
 lecithin :

• Also known as
Phosphatidylcholine
It
nitrogen containing Phospholipid acids
.
in .

a and
P positions esterified with fatty
.
°
are

added tic
•

Phosphoric acid wi third to

to position form Phosphatic
acid .

• The molecule y lecithin exist as

Lovitt onions ( pH -
6.7 )
•

Phospholipase →
Hydrolyze phospholipids .

tip me
lecithin
Lecithin Ly so + FA

choline
de a' thin -1¥
Acyl glycan phosphoryl FA
t

Dipalmitoyl Lecithin Constituent a

lung surfactants .

•
lecithin
Sphingomyelin
-

( ) Ratio
g
L s
Amniotic fluid
g fetal maturity
determines in den .

Ration full
buy maturity
.
-
-
2 → .

② Med Notes (med notes in) .

* Revision Notes med notes site

company
-
. .

[ App Available ]