#Question id: 721
#Unit 1. Molecules and their Interaction Relevant to Biology
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:
#Question id: 720
#Unit 1. Molecules and their Interaction Relevant to Biology
How would a homopolymer of alanine be more likely to form an alpha helix in water or in a hydrophobic medium?
#Question id: 719
#Unit 1. Molecules and their Interaction Relevant to Biology
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: 718
#Unit 1. Molecules and their Interaction Relevant to Biology
Poly- L -leucine in an organic solvent such as dioxane is a helical, whereas poly- L isoleucine is not. Why do these amino acids with the same number and kinds of atoms have different helix-forming tendencies?
#Question id: 717
#Unit 1. Molecules and their Interaction Relevant to Biology
What is Φ & Ψ angles for collagen triple helix?
#Question id: 716
#Unit 1. Molecules and their Interaction Relevant to Biology
In beta turns which amino acid is not allowed at i and i+3 position?