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The interaction between phenylalanine rings in proteins
Open accessAbstract
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.
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Cited by
McGaughey, G. B., Gagné, M., & Rappé, A. K. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.25.15458 · Cited by 1,160
Luscombe, N. M. (2001) · Nucleic Acids Research · doi:10.1093/nar/29.13.2860 · Cited by 981
Amino‐aromatic interactions in proteins
Burley, S. K., & Petsko, G. A. (1986) · FEBS Letters · doi:10.1016/0014-5793(86)80730-x · Cited by 759
Knowledge-based prediction of protein structures and the design of novel molecules
Blundell, T. L., Sibanda, B. L., Sternberg, M. J. E., & Thornton, J. M. (1987) · Nature · doi:10.1038/326347a0 · Cited by 649
Self-citationHunter, C. A., Singh, J., & Thornton, J. M. (1991) · Journal of Molecular Biology · doi:10.1016/0022-2836(91)90271-7 · Cited by 640
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Metadata
- Authors
- Singh, J., & Thornton, J. M.
- Venue
- FEBS Letters
- Publisher
- Wiley
- Published
- 1985-10-21
- Volume
- 191
- Issue
- 1
- Pages
- 1-6
- ISSN
- 0014-5793 (ISSN-L)
- 1873-3468
- OpenAlex
- W2042259662
- Cited by
- 219
- References
- 0
- FWCI
- 2.33
- Type
- journal article
- Language
- en
- Open access
- bronze
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