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Local and macroscopic electrostatic interactions in single α-helices

Research output: Contribution to journalArticle

Original languageEnglish
Pages (from-to)221-228
Number of pages8
JournalNature Chemical Biology
Volume11
Issue number3
Early online date9 Feb 2015
DOIs
DateAccepted/In press - 1 Dec 2014
DateE-pub ahead of print - 9 Feb 2015
DatePublished (current) - Mar 2015

Abstract

The noncovalent forces that stabilize protein structures are not fully understood. One way to address this is to study equilibria between unfolded states and α-helices in peptides. Electrostatic forces - which include interactions between side chains, the backbone and side chains, and side chains and the helix macrodipole - are believed to contribute to these equilibria. Here we probe these interactions experimentally using designed peptides. We find that both terminal backbone-side chain and certain side chain-side chain interactions (which include both local effects between proximal charges and interatomic contacts) contribute much more to helix stability than side chain-helix macrodipole electrostatics, which are believed to operate at larger distances. This has implications for current descriptions of helix stability, the understanding of protein folding and the refinement of force fields for biomolecular modeling and simulations. In addition, this study sheds light on the stability of rod-like structures formed by single α-helices, which are common in natural proteins such as non-muscle myosins.

Additional information

Corrected after print 5 June 2015: http://www.nature.com/nchembio/journal/v11/n9/full/nchembio0915-741e.html

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  • Full-text PDF (accepted author manuscript)

    Rights statement: This is the author accepted manuscript (AAM). The final published version (version of record) is available online via Nature at http://www.nature.com/nchembio/journal/v11/n3/full/nchembio.1739.html. Please refer to any applicable terms of use of the publisher.

    Accepted author manuscript, 381 KB, PDF document

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