PACKING OF ALPHA-HELICES IN GLOBULAR-PROTEINS - LAYER-STRUCTURE OF GLOBIN HYDROPHOBIC CORES

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. © 1979.