Targeting the protein folding transition state by mutation: Large scale (un)folding rate accelerations without altering native stability

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dc.contributor.affiliation000000041762408X
dc.contributor.affiliationInstituto Madrileño de Estudios Avanzados en Nanociencia (IMDEA Nanociencia), Madrid, Spain; Unidad de Nanobiotecnología Asociada al Centro Nacional de Biotecnología (CSIC), Madrid, Spain; Department of Bioengineering, University of California, Merced, CA, United States; Center for Cellular and Biomolecular Machines, University of California, Merced, CA, United Statesen
dc.contributor.authorCampos L.A.
dc.contributor.authorMuñoz V.
dc.date.accessioned2024-09-05T10:43:18Z
dc.date.available2024-09-05T10:43:18Z
dc.date.issued2024
dc.format.mimetypeapplication/pdf
dc.identifier.doi10.1002/pro.5031
dc.identifier.urihttps://hdl.handle.net/20.500.12614/3721
dc.issue.numbere5031
dc.journal.titleProtein Science
dc.language.isoen
dc.relation.projectIDTEMPThe research described in this article was supported by grants: ERC\u20102012\u2010ADG\u2010323059 (European Research Council), MCB\u20102112710 (National Science Foundation) and HRD\u20102112675 (National Science Foundation).
dc.rightsAtribucion-NoComercial-SinDerivadas 3.0 España *
dc.rights.accessRightsopen access
dc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/3.0/es/*
dc.titleTargeting the protein folding transition state by mutation: Large scale (un)folding rate accelerations without altering native stability
dc.typeresearch article
dc.type.hasVersionVoR
dc.volume.number33

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