Hydrogen bonds with π-acceptors in proteins: frequencies and role in stabilizing local 3D structures11Edited by R. Huber

Autor: Gertraud Koellner, Thomas Steiner
Rok vydání: 2001
Předmět:
Zdroj: Journal of Molecular Biology. 305:535-557
ISSN: 0022-2836
DOI: 10.1006/jmbi.2000.4301
Popis: A comprehensive structural analysis of X--H...pi hydrogen bonding in proteins is performed based on 592 published high-resolution crystal structures (< or = 1.6 A). All potential donors and acceptors are considered, including acidic C--H groups. The sample contains 1311 putative X--H...pi hydrogen bonds with N--H, O--H or S--H donors, that is about one per 10.8 aromatic residues. By far the most efficient pi-acceptor is the side-chain of Trp, which accepts one X--H...pi hydrogen bond per 5.7 residues. The focus of the analysis is on recurrent structural patterns involving regular secondary structure elements. Numerous examples are found where peptide X--H...pi interactions are functional in stabilization of helix termini, strand ends, strand edges, beta-bulges and regular turns. Side-chain X--H...pi hydrogen bonds are formed in considerable numbers in alpha-helices and beta-sheets. Geometrical data on various types of X--H...pi hydrogen bonds are given.
Databáze: OpenAIRE