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C-H···O bonds may not stabilize proteins after all A new study calls into question the role of the nontraditional C-H···O hydrogen bonds commonly observed in protein structures. Such C-H···O hydrogen bonds--in which a backbone C-H interacts with an oxygen atom elsewhere in the protein--are thought to be weaker than traditional hydrogen bonds. Still, the prevalence of such contacts has led some scientists to suggest that they may play an important role in stabilizing protein structures. Structural biologist James U. Bowie and his colleagues at the University of California, Los Angeles, have now provided the first experimental test of the strength of a C-H···O hydrogen bond [J. Am. Chem. Soc., published online Feb. 3, http://dx.doi.org/10.1021/ja0317574]. Using a C-H···O hydrogen bond in the membrane protein bacteriorhodopsin as a case study, Bowie and his coworkers measured the thermodynamic stability of versions of the protein containing mutations that disrupt this nontraditional hydrogen bond. They conclude that this and many other C-H···O hydrogen bonds don't make significant contributions to the stability of proteins. Instead, Bowie suggests, many C-H···O contacts may simply facilitate protein packing |
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