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dc.contributor.authorNewberry, Robert W.
dc.contributor.authorRaines, Ronald T
dc.date.accessioned2020-11-20T19:08:55Z
dc.date.available2020-11-20T19:08:55Z
dc.date.issued2019-06
dc.identifier.issn1554-8929
dc.identifier.issn1554-8937
dc.identifier.urihttps://hdl.handle.net/1721.1/128549
dc.description.abstract© 2019 American Chemical Society. A complete inventory of the forces governing protein folding is critical for productive protein modeling, including structure prediction and de novo design, as well as understanding protein misfolding diseases of clinical significance. The dominant contributors to protein folding include the hydrophobic effect and conventional hydrogen bonding, along with Coulombic and van der Waals interactions. Over the past few decades, important additional contributors have been identified, including C-H···O hydrogen bonding, n→π∗ interactions, C5 hydrogen bonding, chalcogen bonding, and interactions involving aromatic rings (cation-π, X-H···π, π-π, anion-π, and sulfur-arene). These secondary contributions fall into two general classes: (1) weak but abundant interactions of the protein main chain and (2) strong but less frequent interactions involving protein side chains. Though interactions with high individual energies play important roles in specifying nonlocal molecular contacts and ligand binding, we estimate that weak but abundant interactions are likely to make greater overall contributions to protein folding, particularly at the level of secondary structure. Further research is likely to illuminate additional roles of these noncanonical interactions and could also reveal contributions yet unknown.en_US
dc.description.sponsorshipNIH (Grant R01-GM044783)en_US
dc.language.isoen
dc.publisherAmerican Chemical Society (ACS)en_US
dc.relation.isversionofhttp://dx.doi.org/10.1021/acschembio.9b00339en_US
dc.rightsArticle is made available in accordance with the publisher's policy and may be subject to US copyright law. Please refer to the publisher's site for terms of use.en_US
dc.sourcePMCen_US
dc.titleSecondary Forces in Protein Foldingen_US
dc.typeArticleen_US
dc.identifier.citationNewberry, Robert W. and Ronald T. Raines. "Secondary Forces in Protein Folding." ACS Chemical Biology 14, 8 (June 2019): 1677–1686 © 2019 American Chemical Societyen_US
dc.contributor.departmentMassachusetts Institute of Technology. Department of Chemistryen_US
dc.relation.journalACS Chemical Biologyen_US
dc.eprint.versionAuthor's final manuscripten_US
dc.type.urihttp://purl.org/eprint/type/JournalArticleen_US
eprint.statushttp://purl.org/eprint/status/PeerRevieweden_US
dc.date.updated2020-11-19T17:53:33Z
dspace.orderedauthorsNewberry, RW; Raines, RTen_US
dspace.date.submission2020-11-19T17:53:35Z
mit.journal.volume14en_US
mit.journal.issue8en_US
mit.licensePUBLISHER_POLICY


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