#Question id: 2272
#Part-A Aptitude & General Biotechnology
Bacteria may be propelled by
#Question id: 13078
#Part-A Aptitude & General Biotechnology
#Question id: 5537
#Part-B Specialized Branches in Biotechnology
The segmented blocks of tissue that develop on each side of the notochord are called the
#Question id: 21005
#Part-B Specialized Branches in Biotechnology
#Question id: 721
#Part-B Specialized Branches in Biotechnology
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: