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.
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