C—H⋯O Hydrogen Bonds in β-sheets
Acta Crystallographica Section D
Volume 53, Issue 3, pages 316–320, May 1997
How to Cite
Fabiola, G. F., Krishnaswamy, S., Nagarajan, V. and Pattabhi, V. (1997), C—H⋯O Hydrogen Bonds in β-sheets. Acta Crystallographica D, 53: 316–320. doi: 10.1107/S0907444997000383
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A detailed analysis of the occurrence of the C—H⋯O hydrogen bonds in sheet regions of proteins has been presented. 11 unique protein structures with resolution 1.3 Å containing β-sheets show a widespread presence of C—H⋯O hydrogen bonds. These have average Cα⋯O, CH⋯O distances and a Cα—H⋯O angle of 3.29, 2.38 Å and 143°, respectively. As in the case of N—H⋯O hydrogen bonds, parallel and antiparallel β-sheet regions show the same hydrogen-bond geometry. An inverse correlation is observed between the hydrogen-bond geometries involving the Cαi—H⋯O=C and the Ni+1—H⋯O=C suggesting that C—H⋯O hydrogen bonds may act as an additional stabilizing factor. The propensity of different amino-acid residues to form such hydrogen bonds varies and shows a clear preference for valine and threonine. C—H⋯O hydrogen bonds involving side chains also occur extensively in β-sheet regions.