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Biomolecules Class Notes

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7 views20 pages

Biomolecules Class Notes

Uploaded by

sabasegowda2912
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© © All Rights Reserved
We take content rights seriously. If you suspect this is your content, claim it here.
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Primary structure ::

It is referees to the linear sequence of amino acids in protein molecule.


The sequence of amino acid that is the positional information in the protein which is the rst amino acid which
is second and so on is called primary structure of Protein

Secondary structure ::
Secondary structure It is formed by folding of primary structure . Now how primary structure undergoes folding , there
are 3 ways
1. Alpha helix ::
Where protein chain undergo right handed coiling.
Pitch is of 5. 4 A.
There are 3 and half amino acids in each turn.
This structure is stabilised by intra molecular hydrogen bond .
Hydrogen bond is formed between NH and carbonyl group .

Examples :: Alpha keratin ( hair Nails . Epidermis )


Myosin , Tropomyosin , Fibrin

Note :: In proteins, only right handed helix is observed .


2. Beta pleated ::
In beta pleated secondary structure two or more polypeptides chain get interconnected by hydrogen bonds in parallel
and anti parallel manner .
A sheath is formed instead of bre or rod in alpha helix .
Two or more proteins are held together by inter hydrogen bonding .
Therefore this secondary structure is also called pleated sheath or beta pleated sheath.

If adjacent strands of polypeptide may run in the same direction , it is parallel beta sheath .
Eg Beta keratin { scales of reptiles , feathers of the birds }

If adjacent strands of polypeptide may run in opposite or. anti parallel direction .
Eg. FIBROIN OF SILK .

Note ::
Hardness of keratin is due to abundance of cysteine amino acid in its structure .

These 2 alpha and beta rst studied by Linus Pauling .

Tertiary structure ::

Quaternary structure ::
Lipids make 18 to 25% of body mass in lean adults .
>Lipids are generally called fats.
>Lipid consist of carbon hydrogen oxygen same as like carbohydrates .
> But in case of lipids content of oxygen is always less as compare to hydrogen and carbon.
>The general formula of carbohydrates is Cn H2N On .
> For eg. General formula of saturated fatty acids is Cn H2N 02..
General formula of unsaturated fatty acids Cn H2N-2xO2.
>Many lipids contain small amount additional elements like phosphorous , nitrogen , sulphur etc.
> Lipids are insoluble in water .
But soluble in non polar solvents like ether , benzene , chloroform , acetone etc .

Lipids are made up of fatty acids + alcohol .


Adenosine triphosphate ::

Phosphodiester bond ::
DNA is negatively charged .
In 1953 Watson and crick proposed the three dimensional structure of DNA .
For discovery of DNA they are awarded with Nobel prize.
Watson and Crick model shows that DNA is double helix with sugar and phosphate back bone on the outside
and paired bases on the inside .
Double helix execute turn after every 10 base pairs . { in case of B DNA )

The pitch of helix is 34A* . Or 3. 4 nm


The diameter of helix is 20A*
The two strands of the DNA are anti parallel to each other . One of the strand runs in 5’to 3’ direction and
other 3’ to 5’
And the double helix is right handed .

Both strand of DNA are held together by hydrogen bonds .


These hydrogen bonds are present between the nitrogenous bases of the both strands .
ADENINE binds to thymine by double hydrogen bonds .
Cytosine binds to the guanine with triple hydrogen bonds .
In one turn there are 10 base pairs are present .The distance between two base pairs is 3 .4 A* or
0.34 nm.
So 3. 4 x 10 = 34A*

Back bone of DNA is formed by sugar and phosphate .


These chains with every nucleotide attached , it shifts slightly by 36 degree .
And when there will be 10 bases completed , that makes the one complete turn of helix or 360 degree .
> This whole speci cation which is given above is for B DNA .

Question > A double stranded DNA OF LENGTH


13.6 nm 20% adenine . How many guanine residue
present ?
Ans > 13 .4 nm = 4 turns of DNA
Because pitch of one turn is 3.4 nm . So base are
80 . As each turn contain 10 base pairs . So number
of base pairs 40 . And bases are 80 .
Adenine is 20 % of 80 .
Each enzyme has an enzyme commission number or code EC.
This is four digit number .
For eg 2. 7. 1. 1 First digit denotes class .
By just seeing rst number we can decide that any particular enzyme belongs to which class .
Classes are further subdivided into subclasses . This number can exist in two digits .
Each subclass is further divided into subdivision .
Last number indicates reaction catalysed by an enzyme .
So E.C number is unique for each enzyme .

Remember enzyme starts its activity at 0 degree Celsius .


And enzymes remain active with in narrow range of temperature .
The temperature at which enzyme show its highest activity is called optimum temperature.
For eg For human optimum temperature is 37 degree Celsius .
And when temperature go above 40 degree Celsius, the slowly weak bonds of enzyme protein start breaking
like ionic bond , hydrophobic bonds etc .
As a result the activity of enzyme start decreasing . And at temp 50 degree Celsius enzymes get denatured .
The temperature below 0 degree Celsius , inactive the enzyme ,

But there are some exceptions where enzyme remain active at very high temperature also .
Eg . Taq polymerase enzyme obtained from thermus aquaticus bacteria found in hot springs .

Now what is Temperature coe cient ??


The term enzyme was coined by Kuhne.
Enzymes are mostly proteins in nature . Except ribozyme and ribonuclease .

Def. of enzyme inhibition ::


Reduction or stoppage of enzyme activity due to presence of adverse condition or chemicals is called enzyme
inhibition .
Any substance that can diminish the velocity of an enzyme catalysed reaction is called inhibitor.

:: Types of inhibition ::
Reversible and irreversible
Competitive and non competitive
Reversible inhibitors bind to enzyme through non covalent bonds . They are of temporary nature . Dilution and dialysis
reduces or eliminates the e ect of reversible inhibition .

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