Abstract
The packing of α-helices is considered in this paper. It is shown that close packing of hydrophobic side-chains on the surface of an individual α-helix or on the surface of the bihelical structure is obtained at a certain combination of rotational isomers. This allows the prediction of rotational isomers in α-helical regions of proteins. The theoretical analysis has been verified with cytochrome c and four globins. The results of theoretical prediction are in good agreement with experimental observation.
Full Text 
Sign-in/Register to access full text options
Sign-in/Register to access full text options 
Paper version not known
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a call
