The interaction between phenylalanine rings in proteins

FEBS Letters

Singh, J.¹  Thornton, J.M.¹ 

[1] Laboratory of Molecular Biology, Crystallography Department, Birkbeck College, Malet Street, London WC1E 7HX, England

关键词: Aromatic-aromatic interaction;    Phenylalanine-phenylalanine interaction;    Protein structure;    Protein stability;    Drug design;   

DOI  :  10.1016/0014-5793(85)80982-0

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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, Tθ, Tϕ 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 Tθ 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.

【 授权许可】

Unknown