A helical conformation of a polypeptide chain, usually right-handed, with maximal intrachain hydrogen bonding; one of the most common secondary structures in proteins.
Through studies on the fluorescence quenching of P3’–P6’ by Rubredoxin, the extent of quenching was found to be stronger in the polymer with more typical features of helix conformation.
For the reason why optical activity of mesomer is counteracted classical answer was not convincing. By use of the helix theory and stable staggered conformation answer can be obtained.
It was found that the compounds are adsorbed on the Ag surface through the carboxyl oxygen atoms, the benzene adopts acclivitous conformation, others lie low on the Ag surface.
Nuclear magnetic resonance techniques are used to determine the national aleutric acid preferential conformation. The results show that the dithionic hydroxyl radicals are in reciprocal cross bearing.