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dc.contributor.authorYunqi, Li
dc.contributor.authorZhang, Jian
dc.contributor.authorTai, David
dc.contributor.authorMiddaugh, C. Russell
dc.contributor.authorZhang, Yang
dc.contributor.authorFang, Jianwen
dc.date.accessioned2017-04-05T18:33:21Z
dc.date.available2017-04-05T18:33:21Z
dc.date.issued2012-01
dc.identifier.citationLi, Y., Zhang, J., Tai, D., Middaugh, C. R., Zhang, Y., & Fang, J. (2012). PROTS: A fragment based protein thermo-stability potential. Proteins, 80(1), 81–92. http://doi.org/10.1002/prot.23163en_US
dc.identifier.urihttp://hdl.handle.net/1808/23573
dc.description.abstractDesigning proteins with enhanced thermo-stability has been a main focus of protein engineering because of its theoretical and practical significance. Despite extensive studies in the past years, a general strategy for stabilizing proteins still remains elusive. Thus effective and robust computational algorithms for designing thermo-stable proteins are in critical demand. Here we report PROTS, a sequential and structural four-residue fragment based protein thermo-stability potential. PROTS is derived from a non-redundant representative collection of thousands of thermophilic and mesophilic protein structures and a large set of point mutations with experimentally determined changes of melting temperatures. To the best of our knowledge, PROTS is the first protein stability predictor based on integrated analysis and mining of these two types of data. Besides conventional cross validation and blind testing, we introduce hypothetical reverse mutations as a means of testing the robustness of protein thermo-stability predictors. In all tests, PROTS demonstrates the ability to reliably predict mutation induced thermostability changes as well as classify thermophilic and mesophilic proteins. In addition, this white-box predictor allows easy interpretation of the factors that influence mutation induced protein stability changes at the residue level.en_US
dc.publisherWileyen_US
dc.rightsThis is the peer reviewed version of the following article: Proteins, which has been published in final form at http://dx.doi.org/10.1002/prot.23163. This article may be used for non-commercial purposes in accordance with Wiley Terms and Conditions for Self-Archiving.en_US
dc.subjectProtein stabilityen_US
dc.subjectThermophilicen_US
dc.subjectPredictionen_US
dc.subjectDataminingen_US
dc.subjectThermostability poteintialen_US
dc.titlePROTS: A fragment based protein thermo-stability potentialen_US
dc.typeArticleen_US
kusw.kuauthorLi, Yunqi
kusw.kuauthorTai, David
kusw.kuauthorMiddaugh, C. Russell
kusw.kuauthorFang, Jianwen
kusw.kudepartmentPharmaceutical Chemistryen_US
dc.identifier.doi10.1002/prot.23163en_US
dc.identifier.orcidhttps://orcid.org/0000-0002-5190-3037
kusw.oaversionScholarly/refereed, author accepted manuscripten_US
kusw.oapolicyThis item meets KU Open Access policy criteria.en_US
dc.rights.accessrightsopenAccess


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