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#Question id: 719
#Part-B Specialized Branches in Biotechnology
Suppose that a 40-residue segment of a protein folds into a two-stranded antiparallel β structure with a 4-residue hairpin turn. What is the longest dimension of this motif?
#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: