Journal of Molecular Biology
Letter to the editorIntrahelical hydrogen bonding of serine, threonine and cysteine residues within α-helices and its relevance to membrane-bound proteins☆
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2022, Advances in Protein Chemistry and Structural BiologyCitation Excerpt :Such a carboxylate-hydroxyl H-bond motif could couple protonation change to changes in local helix dynamics, which can then propagate to remote regions of the protein: The protonation state of the carboxylate group impacts the strength of its inter-helical H-bond to the Ser/Thr hydroxyl group, which in turn influences the availability of the hydroxyl group to engage in intra-helical H-bonding to a backbone carbonyl group (Bondar & Smith, 2017). Intra-helical H-bonding of Ser/Thr to the i-4 backbone carbonyl group of the preceding helical turn is common in α-helical proteins, as it lowers the energetic cost associated with inserting the hydrophilic sidechain into the membrane (Gray & Matthews, 1984). Depending on the sequence-structure context, intra-helical H-bonding between a Ser/Thr hydroxyl and a protein backbone group can associate with enhanced local dynamics of the helix, or with enhanced local hydration (del Val et al., 2012).
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The work was supported in part by grants from the National Institutes of Health (GM20066; GM21967), the National Science Foundation (PCM-8014311) and the M. J. Murdock Charitable Trust. T.M.G. was supported by an NSF graduate fellowship.