Hydrogen Bonding in High-Resolution Protein Structures: A New Method To Assess NMR Protein Geometry

J. Am. Chem. Soc., 124 (35), 10621 -10626, 2002. 10.1021/ja020676p S0002-7863(02)00676-5
Web Release Date: August 8, 2002

Hydrogen Bonding in High-Resolution Protein Structures: A New Method To Assess NMR Protein Geometry

Rebecca S. Lipsitz, Yugal Sharma, Bernard R. Brooks, and Nico Tjandra*

Contribution from the Laboratory of Biophysical Chemistry, Building 50, Room 3503, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, Maryland 20892-8013

Received May 10, 2002

Revised Manuscript Received July 16, 2002

Abstract:

An analysis of backbone hydrogen bonds has been performed on nine high-resolution protein X-ray crystal structures. Backbone hydrogen-bond geometry is compared in the context of X-ray crystal structure resolution. A strong correlation between the hydrogen-bond distance, R_HO, and the hydrogen-bond angle, _NHO, is observed when the X-ray crystal structure resolution is <1.00 Å. Ab initio calculations were performed to substantiate these results. The angle and distance limits found in our correlation for the backbone hydrogen-bond geometry can be used to evaluate the quality of protein structures and for further NMR structure refinement.

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