Crystal Environments and Geometries of Leucine, Isoleucine, Valine, and Phenylalanine Provide Estimates of Minimum Nonbonded Contact and Preferred van der Waals Interaction Distances

Robert O. Gould, Alexandra M. Gray, Paul Taylor, Malcolm D. Walkinshaw*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review


Minimum and optimum nonbonded contact distances have been determined for nonpolar side chains of amino acids. From the Cambridge Crystallographic Data Base, 110 crystal structures containing valine, leucine, isoleucine, or phenylalanine have been analyzed. Minimum contact distances are as follows: C.C = 3.41, C.O = 3.34, C.H = 2.68, H.O = 2.48, H.H = 2.17, all ± 0.05 A. The preferred interatomic separations are 0.3-0.5 A higher than these. Phenyl rings show preferred orientations relative both to other rings and to oxygen atoms in their environment.

Original languageFrench
Pages (from-to)5921-5927
Number of pages7
JournalJournal of the American Chemical Society
Issue number21
Publication statusPublished - Oct 1985

Cite this