An orientation-dependent hydrogen bonding potential improves prediction of specificity and structure for proteins and protein-protein complexes

JOURNAL OF MOLECULAR BIOLOGY

卷:326

Article

Kortemme, T ; Morozov, AV ; Baker, D

关键词: hydrogen bond;    electrostatics;    protein docking;    protein design;    free energy function;   

DOI  :  10.1016/S0022-2836(03)00021-4

来源: Elsevier

【 摘 要 】

Hydrogen bonding is a key contributor to the specificity of intramolecular and intermolecular interactions in biological systems. Here, we develop an orientation-dependent hydrogen bonding potential based on the geometric characteristics of hydrogen bonds in high-resolution protein crystal structures, and evaluate it using four tests related to the prediction and design of protein structures and protein-protein complexes. The new potential is superior to the widely used Coulomb model of hydrogen bonding in prediction of the sequences of proteins and protein-protein interfaces from their structures, and improves discrimination of correctly docked protein-protein complexes from large sets of alternative structures. (C) 2003 Elsevier Science Ltd. All rights reserved.

【 授权许可】

Free