Frequent side chain methyl carbon‐oxygen hydrogen bonding in proteins revealed by computational and stereochemical analysis of neutron structures |
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Authors: | Charles L. Brooks III Raymond C. Trievel |
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Affiliation: | 1. Department of Biophysics, University of Michigan, Ann Arbor, Michigan;2. Department of Chemistry, University of Michigan, Ann Arbor, Michigan;3. Department of Biological Chemistry, University of Michigan, Ann Arbor, Michigan |
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Abstract: | The propensity of backbone Cα atoms to engage in carbon‐oxygen (CH···O) hydrogen bonding is well‐appreciated in protein structure, but side chain CH···O hydrogen bonding remains largely uncharacterized. The extent to which side chain methyl groups in proteins participate in CH···O hydrogen bonding is examined through a survey of neutron crystal structures, quantum chemistry calculations, and molecular dynamics simulations. Using these approaches, methyl groups were observed to form stabilizing CH···O hydrogen bonds within protein structure that are maintained through protein dynamics and participate in correlated motion. Collectively, these findings illustrate that side chain methyl CH···O hydrogen bonding contributes to the energetics of protein structure and folding. Proteins 2015; 83:403–410. © 2014 Wiley Periodicals, Inc. |
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Keywords: | CH· · · O C H· · · O CH O CH· · · O C H· · · O hydrogen bond neutron structure molecular dynamics quantum mechanics |
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