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The geometries of interacting arginine‐carboxyls in proteins
Author(s) -
Singh J.,
Thornton J.M.,
Snarey M.,
Campbell S.F.
Publication year - 1987
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(87)80441-6
Subject(s) - arginine , chemistry , biochemistry , computational biology , computational chemistry , amino acid , biology
The geometries are reported for interacting arginine‐carboxyl pairs obtained from 37 high resolution protein structures solved to a resolution of 2.0 Å or better. The closest interatomic distance between the guanidinium and carboxyl is less than 4.2 Å for 74 arginine and carboxyl groups, with the majority of these lying within hydrogen‐bonding distance (2.6–3.0 Å). Interacting pairs have been transformed into a common orientation, and arginine‐carboxyl, and carboxyl‐arginine geometries have been calculated. This has been defined in terms of the spherical polar angles T θ, T ϕ, and the angle P , between the guanidinium and carboxyl planes. Results show a clear preference for the guanidinium and carboxyl groups to be approximately coplanar, and for the carboxyl oxygens to hydrogen bond with the guanidinium nitrogens. Single nitrogen‐single oxygen is the most common type of interaction, however twin nitrogen‐twin oxygen interactions also occur frequently. The majority of these occur between the carboxyl oxygens and the NH1 and NE atoms of the arginine. and are only rarely observed for NH1 and NH2. The information presented may be of use in the modelling of arginine‐carboxyl interactions within proteins.