Hydrogen bonding in high-resolution protein structures: a new method to assess NMR protein geometry |
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Authors: | Lipsitz Rebecca S Sharma Yugal Brooks Bernard R Tjandra Nico |
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Institution: | Laboratory of Biophysical Chemistry, Building 50, Room 3503, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, Maryland 20892-8013, USA. |
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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, theta(NHO), is observed when the X-ray crystal structure resolution is <1.00 A. 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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