BioMolecules Mind map

1. BIOMOLECULES
PROTEINS
Polymers of amino acids
Class of nitrogenous compounds
large molecules
having one or more long chain
of amino acids
R
H N
3 CH COOH
α carbon
amino
group
+
Carboxyl
group
side
chain
Zwitter ion / dipolar ion
•
•
ionic form when diss slued
in water
Act as proton doner or
proton acceptor
NH3
+
CH
R
COOH NH3
+
CH COO
- H N
2 CH COO
R R
-
Zwitter ion
Basic - lysmi
Acidic amino acid - Glutamic acid Neutral - value
Aromatic amino acid - jyrosine,
phenylalanine and Tryhophan
Essential Amino
acids
Non – essential
amin acids
•
• Can not be synthesised
in the body
Isoleucine, Levine
methionine, Phenylalanine,
Threonine, Tryptophane,
lysine, valvule, Arginine
Histidine
• Synthesized in the
body
Gylanic, Alanis, serine,
aspartic acid,
Asparagine,
cysteine, Glutaric acid,
Glutamine protein,
Tyrosine
Structure of Portion
• Primary structure - sequence of Amino acids,
which are joined by peptide bonds (Add linage)
• Secondary structure - Luige level of portion
organization. eg:- Keratin
α helix:- polypeptide chain twisted into
helical form
β- pleated:- 2 or more polypeptide
chain lime up side by side
• Tertiary structure - Helical polypeptide
chain is folded into a
woolen wall, ex:- myoglobin
• Quaternary structures:- Composed of
two or more polypepted
chains – held together by hydrophobia
issler actions, illetrostalic
interactions & H – bonds , Ex:- Hemoglobin
LIPIDS
Water insoluble
Saturaled fatly acids- No double bonds
Unsaturated fatly acids double bonds
are present
Fatly acid - has a COOH group
attached to an group
Plastic acid – 16 carbons
Arachidonic acid – 20 carbons
Esterified through ester bond
forming mono, di and triglycerides
•
•
•
•
•
•
•
Two or more amino acids
all linked by peptide
NH CH C OH + NH CH COO
3
-
R
O
N C C N C COOH
H
H
H
R O
H
R
H
Peptide
Bond
Holoenzyme
Peptide Bond
Apoenzyme Cofactors
Protein palt non protein
part
Catalytic
activity of
the enzyme
Prosthetic
group
•
•
Tightly bond
to enzyme
Coenzyme
Organic
compounds
not bound
tightly to
apoenzyme
Living tissues are
treated with
trichloro acetic
acid and grind it
to form slurry
Organic molecule
products by living
organisms
Analysis of chemical
composition of
organic Compounds. Proteins nucleic
acids carboh-
ydrates and lipids
are common
biomolecules
Sample of tissue
should be treent
to obtaisi ash.
Composed of
H,O,N,P,S.
Metabohtes
which are etherutilized in
metabolic functions/
synthesised in cellular
machinery
Imetaboliles
sugars, amino acids, fatty
acids nucleosides & nucleoles
2O metabolites
Pigments
Carotenoids and
anthocyanins
Alkaloids
Morphine and
codeine
Terpenoids
Monoterpenes &
diterpenes
Essential oils Lemongrass oil
Toxins Abrin & ricin
Lectins Concanavalin A
Drugs Vinblastine &
curcumin
Polymeric
subs
Rubber, guns &
cellulose
Nucleic
acids
Nucleic acids
DNA (Deoxyribonuclease
acid)
RNA (Ribonucleic acids)
• Polymers of nucleotides
• Adenine (A) & Guanine (G) - Purines,
Cytosine(c), thymine (T) and Uracil (U)
- pyrimidines
Nucleic Acids :- (i) DNA (Deoxyri-
bonuclease acids, (ii) RNA
(Ribonucleic acids)
Nitrogenous
base
Phosphate
group
Pentose
Type of DNA are
• BDNA – common form
of DNA
DNA – helical ladder
like Apairs with
T (A = T), G pairs
with C (G = C)
• ZDNA,
• ADNA,
• CDNA
Nucleosides
Nitrogenous base
+
pentose
Nucleotide - Nucleoside
+ phosphate
Homopotymers
Fructose
(mmo)
inulin
cellulose
– Glucose
chitin
(N- acetyl
glucosamine)
Statch
Glucos
(mono) Glycoger
Polysaccharides
o Starch, cellulose, glycogen
o Carbohydrates with a long chain
of polymers
o Homopolymers (Consist of single
mono- saccharide Units)
Heteropolymers (made of different
monosa charades Units)
Triglycerides
oil (low meting
point)
fats (high
meting points)
Glycerol – Simple amino acids
(Trihydroxy propane)
Lecithin
present in cell membrane
Phospholiprid
Phosphorus + phosphorylated
organic Compound.
Transition state
Activation energy
without enzyme
Activation
energy with enzyme
Product (P)
Potential
Energy
Progress of reaction
Substrate (s)
Vmax
½Vmax
Rate
of
reaction
Km
Substrate concentration [S]
No inhibitor
Competitive inhibitor
No inhibitor
Non-competitive inhibitor
n
o
i
t
c
a
e
r
f
o
e
t
a
R
Vmax
Vmax
Km
Substrate concentration [S]
Non-competitive inhibition
Oxidoreductase
transferases
Hydrolases
lyases
isomerases
ligases
enzyme
classification
Enzymes
Biological
catalyst
Mostly
proteinaceous
except Ribozymes
(nucleic acid)
Activation
• minimous energy
amount of
energy
• required to
activate subs-
trate to a
condition in
which they
can undergo
chemical each
• High or low
temperature
inactivates the
enzyme actively
• pH, & substrali
conch - affect
enzyme actively
Glycosidic bonds link
monosaccharides
Base
O
O
P
O
O
CH2
5‘
3‘
Phosphodiester
bond
Phosphate
O
Base
O
Inorganic chemical
composition
DR. Anand Mani
anand_mani16 https://www.anandmani.com/ https://discord.io/anandmani t.me/anandmani001