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Multiple helical conformations of the helix‐turn‐helix region revealed by NOE‐restrained MD simulations of tryptophan aporepressor, TrpR

Author(s): Harish, Balasubramanian; Swapna, GVT; Kornhaber, Gregory J; Montelione, Gaetano T; Carey, Jannette

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dc.contributor.authorHarish, Balasubramanian-
dc.contributor.authorSwapna, GVT-
dc.contributor.authorKornhaber, Gregory J-
dc.contributor.authorMontelione, Gaetano T-
dc.contributor.authorCarey, Jannette-
dc.date.accessioned2024-08-01T14:00:55Z-
dc.date.available2024-08-01T14:00:55Z-
dc.date.issued2017-01-25en_US
dc.identifier.citationHarish, Balasubramanian, Swapna, GVT, Kornhaber, Gregory J, Montelione, Gaetano T, Carey, Jannette. (2017). Multiple helical conformations of the helix‐turn‐helix region revealed by NOE‐restrained MD simulations of tryptophan aporepressor, TrpR. Proteins: Structure, Function, and Bioinformatics, 85 (4), 731 - 740. doi:10.1002/prot.25252en_US
dc.identifier.issn0887-3585-
dc.identifier.urihttp://arks.princeton.edu/ark:/88435/pr1f18sf6k-
dc.description.abstractThe nature of flexibility in the helix-turn-helix region of E. coli trp aporepressor has been unexplained for many years. The original ensemble of nuclear magnetic resonance (NMR structures showed apparent disorder, but chemical shift and relaxation measurements indicated a helical region. Nuclear Overhauser effect (NOE) data for a temperature-sensitive mutant showed more helical character in its helix-turn-helix region, but nevertheless also led to an apparently disordered ensemble. However, conventional NMR structure determination methods require all structures in the ensemble to be consistent with every NOE simultaneously. This work uses an alternative approach in which some structures of the ensemble are allowed to violate some NOEs to permit modeling of multiple conformational states that are in dynamic equilibrium. Newly measured NOE data for wild-type aporepressor are used as time-averaged distance restraints in molecular dynamics simulations to generate an ensemble of helical conformations that is more consistent with the observed NMR data than the apparent disorder in the previously reported NMR structures. The results indicate the presence of alternating helical conformations that provide a better explanation for the flexibility of the helix-turn-helix region of trp aporepressor.en_US
dc.format.extent731 - 740en_US
dc.languageenen_US
dc.language.isoen_USen_US
dc.relation.ispartofProteins: Structure, Function, and Bioinformaticsen_US
dc.rightsAuthor's manuscripten_US
dc.titleMultiple helical conformations of the helix‐turn‐helix region revealed by NOE‐restrained MD simulations of tryptophan aporepressor, TrpRen_US
dc.typeJournal Articleen_US
dc.identifier.doidoi:10.1002/prot.25252-
dc.identifier.eissn1097-0134-
pu.type.symplectichttp://www.symplectic.co.uk/publications/atom-terms/1.0/journal-articleen_US

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