Hydrophobicity, hydrophilicity, and the radial and orientational distributions of residues in native proteins.

Abstract:

:The radial distributions of the Calpha and side-chain atoms in a sample of 13 native proteins have been examined. It is found that there are substantial differences in behavior between different atoms of the same amino acid. In particular, the Calpha atoms of polar residues show no particular preference for being far from the center of mass. In light of these results, a new criterion for hydrophobicity and hydrophilicity is proposed--namely, the orientational preference of the side chain. The distribution of this property is shown, and it is suggested that this provides a basis for incorporating hydrophobic interactions into a protein folding algorithm.

authors

Rackovsky S,Scheraga HA

doi

10.1073/pnas.74.12.5248

subject

Has Abstract

pub_date

1977-12-01 00:00:00

pages

5248-51

issue

12

eissn

0027-8424

issn

1091-6490

journal_volume

74

pub_type

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