Addition of urea leads to a two-state transition between α-helix and random coil conformation. It has been observed that [θ]222 of the polypeptide is -11000 deg cm2 dmol-1 in the presence of 6M urea. Initially it was observed that tile values of mean residue ellipticity at 220 nm ([θ]220) are -36000, and +4000 deg cm2 dmol-1 for α-helix, and random coil conformations of this polypeptide. The percentage of the polypeptide in α-helix conformation is:

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#Question id: 18663

#Part-A Aptitude & General Biotechnology

When a protein exists in mono-, di- and tri-phosphorylated forms. The difference of a couple of phosphate groups has no significant effect on the overall relative molecular mass of the protein, hence a single band on SDS gels, but the small charge difference introduced on each molecule can be detected by

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#Question id: 18664

#Part-A Aptitude & General Biotechnology

2D electrophoresis is the combination of 

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#Question id: 18665

#Part-A Aptitude & General Biotechnology

In a road accident a forensic scientist collected traces of blood or other biological fluids and he wants to compared samples according to the composition of certain isoenzymes, for this which technique will efficiently work

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#Question id: 18666

#Part-A Aptitude & General Biotechnology

The above figure shows where sample applied was 100 µg of total protein extracted from a normal dog heart ventricle. The first dimension was conducted using a pH 4–7 isoelectric focussing gel. The second dimension was a 12% SDS–PAGE vertical slab gel. The pattern was visualised by silver staining. Which of the following techniques is applied

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#Question id: 18667

#Part-A Aptitude & General Biotechnology

Which of the following is highly sophisticated analytical method for analysing protein mixtures

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#Question id: 18668

#Part-A Aptitude & General Biotechnology

Enzymes and antibody can easily be detected in samples subjected to electrophoresis on cellulose acetate, by using the