Show simple item record

dc.contributor.authorQi, Yifei
dc.contributor.authorIm, Wonpil
dc.date.accessioned2017-05-17T15:24:17Z
dc.date.available2017-05-17T15:24:17Z
dc.date.issued2013-08-13
dc.identifier.citationQi, Y., & Im, W. (2013). Quantification of Drive-Response Relationships Between Residues During Protein Folding. Journal of Chemical Theory and Computation, 9(8), 10.1021/ct4002784. http://doi.org/10.1021/ct4002784en_US
dc.identifier.urihttp://hdl.handle.net/1808/24232
dc.description.abstractMutual correlation and cooperativity are commonly used to describe residue-residue interactions in protein folding/function. However, these metrics do not provide any information on the causality relationships between residues. Such drive-response relationships are poorly studied in protein folding/function and difficult to measure experimentally due to technical limitations. In this study, using the information theory transfer entropy (TE) that provides a direct measurement of causality between two times series, we have quantified the drive-response relationships between residues in the folding/unfolding processes of four small proteins generated by molecular dynamics simulations. Instead of using a time-averaged single TE value, the time-dependent TE is measured with the Q-scores based on residue-residue contacts and with the statistical significance analysis along the folding/unfolding processes. The TE analysis is able to identify the driving and responding residues that are different from the highly correlated residues revealed by the mutual information analysis. In general, the driving residues have more regular secondary structures, are more buried, and show greater effects on the protein stability as well as folding and unfolding rates. In addition, the dominant driving and responding residues from the TE analysis on the whole trajectory agree with those on a single folding event, demonstrating that the drive-response relationships are preserved in the non-equilibrium process. Our study provides detailed insights into the protein folding process and has potential applications in protein engineering and interpretation of time-dependent residue-based experimental observables for protein function.en_US
dc.publisherAmerican Chemical Societyen_US
dc.rightsThis document is the Accepted Manuscript version of a Published Work that appeared in final form in Journal of Chemical Theory and Computation, copyright © American Chemical Society after peer review and technical editing by the publisher. To access the final edited and published work see http://doi.org/10.1021/ct4002784.en_US
dc.subjectInformation theoryen_US
dc.subjectTransfer entropyen_US
dc.subjectMutual informationen_US
dc.subjectMolecular Dynamicsen_US
dc.titleQuantification of Drive-Response Relationships Between Residues During Protein Foldingen_US
dc.typeArticleen_US
kusw.kuauthorQi, Yifei
kusw.kuauthorIm, Wonpil
kusw.kudepartmentMolecular Biosciencesen_US
dc.identifier.doi10.1021/ct4002784en_US
kusw.oaversionScholarly/refereed, author accepted manuscripten_US
kusw.oapolicyThis item meets KU Open Access policy criteria.en_US
dc.identifier.pmidPMC3819712en_US
dc.rights.accessrightsopenAccess


Files in this item

Thumbnail

This item appears in the following Collection(s)

Show simple item record