INTRODUCTION HISTORY PROTEIN CHROMATOGRAPHY ADSORPTION CHROMATOGRAPHY ION EXCHANGE CHROMATOGRAPHY GELFILTRATION CHROMATOGRAPHY AFFINITY CHROMATOGRAPHY ELECTROPHORESIS X-RAY DIFFRACTION NMR SPECTROSCOPY RADIOISOTOPE TRACER TECHNIQUE AUTORADIOGRAPHY CONCLUSION REFRENCES

1. Methods of study of protein
By
KAUSHAL KUMAR SAHU
Assistant Professor (Ad Hoc)
Department of Biotechnology
Govt. Digvijay Autonomous P. G. College
Raj-Nandgaon ( C. G. )

2. synopsis
 INTRODUCTION
 HISTORY
 PROTEIN
 CHROMATOGRAPHY
 ADSORPTION CHROMATOGRAPHY
 ION EXCHANGE CHROMATOGRAPHY
 GELFILTRATION CHROMATOGRAPHY
 AFFINITY CHROMATOGRAPHY
 ELECTROPHORESIS
 X-RAY DIFFRACTION
 NMR SPECTROSCOPY
 RADIOISOTOPE TRACER TECHNIQUE
 AUTORADIOGRAPHY
 CONCLUSION
 REFRENCES

3. INTRODUCTION
 Proteins perform a vast array of functions within
living organisms, including catalyzing metabolic
reactions, replicating DNA, responding to stimuli,
and transporting molecules from one location to
another.
 Source of protein

4. HISTORY
 Tswet, Russian botanist is credicted for the
development of chromatography.
 New forms of chromatography developed in the
1930s and 1940s.
 Nuclear magnetic resonance was first described and
measured in molecular beams by Isidor Rabi in 1938,
and in 1944, and got noble Nobel Prize in physics for
this work.
 Electrophoresis is an electrophoretic phenomenon
by observed in 1907 by Ferdinand Frederic Reuss

5. PROTEINS
 Proteins are large biological molecules consisting of
one or more chains of amino acids. Proteins perform
a vast array of functions within living organisms.
 Proteins differ from each other in the sequence of
aminoacid.

6. CHROMATOGRAPHY:-

7. ADSORPTION CHROMATOGRAPHY:-
 Cell extract is pass
through a column.
 Effluent solution is
collected continuously in
small fraction.
 And fraction ofprotein is
estimated by
spectrophotometer.

8. ION EXCHANGE CHROMATOGRAPHY:-
 In this cellulosic ion
exchange is taken in a
column.
 Which is in the form of
small beads.
 This technique can give
large scale protein
purification.
 Insulin purification.

9. GEL FILTRATION CHROMATOGRAPHY:-
 In this proteins are
separated on the basis of
molecular size.
 Gel sephadex is used.

10. AFFINITY CHROMATOGRAPHY:-
 It is based on enzyme –
substate binding.
 One component of
mixture containing
enzyme binds towards
the solid sopport of
column.

11. ELECTROPHORESIS:-
 Electrophoresis is the motion of dispersed
particles relative to a fluid under the influence of a
spatially uniform electric field.
 It is an electrokinetic phenomenon.
 2- D Electrophoresis.

12. X-ray diffraction :-
 It is an analytical
technique and give
information about the
crystal stucture.
 Based on observing the
scattering intensity of X-
ray beam.

13. NMR SPECTROSCOPY:-
 It is a research technique
that exploits the
magnetic property of
certain atomic nuclei.
 Determines the physical
and chemical properties
of atom. Or the
molecules in which they
are contain

14. RADIOISOTOPE TRACER TECHNIQUE:-
 It is a chemical
compound in which one
or more atoms have been
replaced by a isotopes.
 Used to explore the
mechanism of chemical
reaction.
 Tritium is a example.

15. AUTORADIOGRAPH:-

16. Conclusion
 Thus, we can conclude that by this study we can
detect the chemical nature and the properties of
protein which plays an important role in the cell and
in the biological level.

17. REFRENCES
 Principle of Biochemistry :- David L. Nelson and
Michael M. Cox
 Principles of gene manipulation and genomics : by
primrose and twyman
 Life science: fundamental and practice
 B.D.SINGH (Biotechnology)
 en.wikipedia.org/wiki/protein