Informace o publikaci

Water-tryptophan interactions: lone-pair-pi or O-H-pi? Molecular dynamics simulations of beta-galactosidase suggest that both modes can co-exist

Autoři

DUREC Matúš MAREK Radek KOZELKA Jiří

Rok publikování 2018
Druh Článek v odborném periodiku
Časopis / Zdroj Chemistry - A European Journal
Fakulta / Pracoviště MU

Přírodovědecká fakulta

Citace
www DOI: 10.1002/chem.201705364
Doi http://dx.doi.org/10.1002/chem.201705364
Obor Fyzikální chemie a teoretická chemie
Klíčová slova water; tryptophane; interaction; molecular dynamics
Přiložené soubory
Popis In proteins, the indole side-chain of tryptophan can interact with water molecules either in-plane, forming H-bonds, or out-of-plane, with the water molecule contacting the aromatic pi-face. The latter interaction can be either of the lone-pair---pi (lp---pi) type or correspond to the O-H---pi binding mode, an ambiguity that X-ray structures usually do not resolve. Here we report molecular dynamics (MD) simulations of a solvated beta-galactosidase monomer which illustrate how a water molecule located at the pi-face of an indole side-chain of tryptophan can adapt to the position of proximate residues and "select" its binding mode. In one such site, the water molecule is predicted to rapidly oscillate between the O-H---pi and lp---pi binding modes, gaining thus entropic advantage. Our MD simulations provide support for the role of lp---pi interactions in the stabilization of protein structures.
Související projekty:

Používáte starou verzi internetového prohlížeče. Doporučujeme aktualizovat Váš prohlížeč na nejnovější verzi.

Další info