PMID: 11607570Aug 1, 1995Paper

Significance of bound water to local chain conformations in protein crystals

Proceedings of the National Academy of Sciences of the United States of America
C H Robert, P S Ho

Abstract

We examine how the polypeptide chain in protein crystal structures exploits the multivalent hydrogen-bonding potential of bound water molecules. This shows that multiple interactions with a single water molecule tend to occur locally along the chain. A distinctive internal-coordinate representation of the local water-binding segments reveals several consensus conformations. The fractional water occupancy of each was found by comparison of the total number of conformations in the database regardless of the presence or absence of bound water. The water molecule appears particularly frequently in type II beta-turn geometries and an N-terminal helix feature. This work constitutes a first step into assessing not only the generality but also the significance of specific water binding in globular proteins.

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Citations

Nov 27, 1999·Biochimie·L Debelle, A J Alix
Jan 20, 2005·Bioinformatics·Fred P Davis, Andrej Sali
Aug 11, 2006·Bioinformatics·Aalt D J van Dijk, Alexandre M J J Bonvin
Oct 12, 2000·Biochemical and Biophysical Research Communications·H Reiersen, A R Rees
Nov 29, 2008·Journal of Molecular Biology·Gilleain M TorranceE James Milner-White
Mar 23, 2004·Journal of Molecular Biology·Charles H RobertDavid Perahia
Apr 28, 2005·Proteins·Francis RodierJoël Janin
Dec 8, 2010·Macromolecular Bioscience·David van der SpoelCarl Caleman
Jul 18, 1997·Biochemical and Biophysical Research Communications·E Nishio, Y Watanabe
Sep 14, 2011·The Journal of Physical Chemistry. B·Keith M Krise, Bratoljub H Milosavljevic

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