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The interaction between phenylalanine rings in proteins
Author(s) -
Singh J.,
Thornton J.M.
Publication year - 1985
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(85)80982-0
Subject(s) - phenylalanine , polar , ring (chemistry) , perpendicular , distribution (mathematics) , geometry , preference , chemistry , mathematics , physics , crystallography , stereochemistry , mathematical analysis , quantum mechanics , amino acid , statistics , biochemistry , organic chemistry
An analysis has been made of the geometry of phenylalanine‐phenylalanine interactions in proteins of known structure. 162 Phe‐Phe interactions were found with C‐C distances less than 4.6 Å. Three angles were used to define the geometry of interaction, P = the angle betwen ring planes, and polar coordinates, T θ, T ϕ to specify the relative spatial disposition of the two rings. The overall distribution of P values is the same as that expected for a random distribution of planes in 3 dimensions; i.e. the majority, of interactions have P approaching 90°. However, for high T θ values (when one Phe lies directly above the ring of the other Phe) the distribution is non‐random, and a preference for perpendicular interactions is expressed. This preference is in accord with recent quantum‐mechanical calculations.