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dc.contributor.authorTowse, Clare-Louise*
dc.contributor.authorAkke, M.*
dc.contributor.authorDaggett, V.*
dc.date.accessioned2017-08-30T14:13:43Z
dc.date.available2017-08-30T14:13:43Z
dc.date.issued2017-04-04
dc.identifier.citationTowse C, Akke M and Daggett V (2017) The dynameomics entropy dictionary: a large-scale assessment of conformational entropy across protein fold space. The Journal of Physical Chemistry B. 121(16): 3933-3945.en_US
dc.identifier.urihttp://hdl.handle.net/10454/13021
dc.descriptionYesen_US
dc.description.abstractMolecular dynamics (MD) simulations contain considerable information with regard to the motions and fluctuations of a protein, the magnitude of which can be used to estimate conformational entropy. Here we survey conformational entropy across protein fold space using the Dynameomics database, which represents the largest existing dataset of protein MD simulations for representatives of essentially all known protein folds. We provide an overview of MD-derived entropies accounting for all possible degrees of dihedral freedom on an unprecedented scale. Although different side chains might be expected to impose varying restrictions on the conformational space that the backbone can sample, we found that the backbone entropy and side chain size are not strictly coupled. An outcome of these analyses is the Dynameomics Entropy Dictionary, the contents of which have been compared with entropies derived by other theoretical approaches and experiment. As might be expected, the conformational entropies scale linearly with the number of residues, demonstrating that conformational entropy is an extensive property of proteins. The calculated conformational entropies of folding agree well with previous estimates. Detailed analysis of specific cases identify deviations in conformational entropy from the average values that highlight how conformational entropy varies with sequence, secondary structure, and tertiary fold. Notably, alpha-helices have lower entropy on average than do beta-sheets, and both are lower than coil regions.en_US
dc.description.sponsorshipNational Institutes of Health, US Department of Energy Office of Biological Research, National Energy Research Scientific Computing Center, Swedish Research Council, Knut and Alic Wallenberg Foundationen_US
dc.language.isoenen_US
dc.relation.isreferencedbyhttp://dx.doi.org/10.1021/acs.jpcb.7b00577en_US
dc.rights© 2017 ACS. This document is the Accepted Manuscript version of a Published Work that appeared in final form in The Journal of Physical Chemistry B, copyright American Chemical Society after peer review and technical editing by the publisher. To access the final edited and published work see http://dx.doi.org/10.1021/acs.jpcb.7b00577.en_US
dc.subjectMolecular dynamics simulations; Protein structure; Conformational entropyen_US
dc.titleThe dynameomics entropy dictionary: a large-scale assessment of conformational entropy across protein fold spaceen_US
dc.status.refereedYesen_US
dc.date.application2017-04-04
dc.typeArticleen_US
dc.type.versionAccepted Manuscripten_US


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