Modest stabilization by most hydrogen-bonded side-chain interactions in membrane proteins

Nathan HyunJoong Joh, Andrew Min, Salem Faham, Julian P. Whitelegge, Duan Yang, Virgil L. Woods and James U. Bowie ()
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Nathan HyunJoong Joh: UCLA-DOE Center for Genomics and Proteomics, Molecular Biology Institute
Andrew Min: UCLA-DOE Center for Genomics and Proteomics, Molecular Biology Institute
Salem Faham: and
Julian P. Whitelegge: The NPI-Semel Institute, Pasarow Mass Spec Laboratory, University of California, Los Angeles, California 90095, USA
Duan Yang: UCLA-DOE Center for Genomics and Proteomics, Molecular Biology Institute
Virgil L. Woods: University of California, San Diego, La Jolla, California 92093-0656, USA
James U. Bowie: UCLA-DOE Center for Genomics and Proteomics, Molecular Biology Institute

Nature, 2008, vol. 453, issue 7199, 1266-1270

Abstract: Side-chain stabilization in membrane proteins Hydrogen bonds have been widely assumed to be strongly stabilizing in membrane proteins, but there have been few experimental tests of this notion. In this work, interaction free energies were measured between eight hydrogen-bonded side chains in bacteriorhodopsin. Contrary to expectations, most make only modest stabilizing contributions, averaging 0.6 kcal mol−1. The results suggest that views of membrane protein folding, evolution and function should reflect such weak polar side-chain interactions.

Date: 2008
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DOI: 10.1038/nature06977

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