Please use this identifier to cite or link to this item: https://hdl.handle.net/10356/80215
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dc.contributor.authorGupta, Sebantien
dc.contributor.authorBhattacharjya, Surajiten
dc.date.accessioned2016-04-15T06:57:16Zen
dc.date.accessioned2019-12-06T13:45:05Z-
dc.date.available2016-04-15T06:57:16Zen
dc.date.available2019-12-06T13:45:05Z-
dc.date.issued2014en
dc.identifier.citationGupta, S., & Bhattacharjya, S. (2014). Characterization of the near native conformational states of the SAM domain of Ste11 protein by NMR spectroscopy. Proteins: Structure, Function, and Bioinformatics, 82(11), 2957-2969.en
dc.identifier.issn0887-3585en
dc.identifier.urihttps://hdl.handle.net/10356/80215-
dc.description.abstractThe sterile alpha motif or SAM domain is one of the most frequently present protein interaction modules with diverse functional attributions. SAM domain of the Ste11 protein of budding yeast plays important roles in mitogen-activated protein kinase cascades. In the current study, urea-induced, at subdenaturing concentrations, structural, and dynamical changes in the Ste11 SAM domain have been investigated by nuclear magnetic resonance spectroscopy. Our study revealed that a number of residues from Helix 1 and Helix 5 of the Ste11 SAM domain display plausible alternate conformational states and largest chemical shift perturbations at low urea concentrations. Amide proton (H/D) exchange experiments indicated that Helix 1, loop, and Helix 5 become more susceptible to solvent exchange with increased concentrations of urea. Notably, Helix 1 and Helix 5 are directly involved in binding interactions of the Ste11 SAM domain. Our data further demonstrate that the existence of alternate conformational states around the regions involved in dimeric interactions in native or near native conditions.en
dc.format.extent36 p.en
dc.language.isoenen
dc.relation.ispartofseriesProteins: Structure, Function, and Bioinformaticsen
dc.rights© 2014 Wiley Periodicals, Inc. This is the author created version of a work that has been peer reviewed and accepted for publication by Proteins: Structure, Function, and Bioinformatics, Wiley Periodicals, Inc.. It incorporates referee’s comments but changes resulting from the publishing process, such as copyediting, structural formatting, may not be reflected in this document. The published version is available at: [http://dx.doi.org/10.1002/prot.24652].en
dc.subjectNuclear magnetic resonanceen
dc.subjectLow-energy alternate statesen
dc.subjectNear-native conformationsen
dc.subjectSte11 SAM domainen
dc.titleCharacterization of the near native conformational states of the SAM domain of Ste11 protein by NMR spectroscopyen
dc.typeJournal Articleen
dc.contributor.schoolSchool of Biological Sciencesen
dc.identifier.doi10.1002/prot.24652en
dc.description.versionAccepted versionen
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item.grantfulltextopen-
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