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dc.contributor.author
Sánchez Miguel, Ignacio Enrique
dc.contributor.author
Ferreiro, Diego
dc.contributor.author
de Prat Gay, Gonzalo
dc.date.available
2017-04-12T20:01:07Z
dc.date.issued
2011-01
dc.identifier.citation
Sánchez Miguel, Ignacio Enrique; Ferreiro, Diego; de Prat Gay, Gonzalo; Mutational analysis of kinetic partitioning in protein folding and protein-DNA binding; Oxford University Press; Protein Engineering Design & Selection; 24; 1-2; 1-2011; 179-184
dc.identifier.issn
1741-0126
dc.identifier.uri
http://hdl.handle.net/11336/15240
dc.description.abstract
Kinetic partitioning between competing routes is present in many biological processes. Here, we propose a methodology to characterize kinetic partitioning through site-directed mutagenesis and apply it to parallel routes for unfolding of the TI I27 protein and for recognition of its target DNA by the human papillomavirus E2 protein. The balance between the two competing reaction routes can be quantified by the partitioning constant K(p). K(p) is easily modulated by point mutations, opening the way for the rational design of kinetic partitioning. Conserved wild-type residues strongly favor one of the two competing reactions, suggesting that in these systems there is an evolutionary pressure to shift partitioning towards a certain route. The mutations with the largest effects on partitioning cluster together in space, defining the protein regions most relevant for the modulation of partitioning. Such regions are neither fully coincident with nor strictly segregated from the regions that are important from each competing reaction. We dissected the mutational effects on partitioning into the contributions from each competing route using a new parameter called pi-value. The results suggest how the design of kinetic partitioning may be approached in each case.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
Oxford University Press
dc.rights
info:eu-repo/semantics/openAccess
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.subject
Kinetic Partitioning
dc.subject
Point Mutation
dc.subject
Protein Design
dc.subject
Protein-Dna Binding
dc.subject.classification
Biofísica
dc.subject.classification
Ciencias Biológicas
dc.subject.classification
CIENCIAS NATURALES Y EXACTAS
dc.title
Mutational analysis of kinetic partitioning in protein folding and protein-DNA binding
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2017-03-29T14:45:37Z
dc.journal.volume
24
dc.journal.number
1-2
dc.journal.pagination
179-184
dc.journal.pais
Reino Unido
dc.journal.ciudad
Oxford
dc.description.fil
Fil: Sánchez Miguel, Ignacio Enrique. Fundación Instituto Leloir; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquimicas de Buenos Aires; Argentina. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina
dc.description.fil
Fil: Ferreiro, Diego. Fundación Instituto Leloir; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquimicas de Buenos Aires; Argentina. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina
dc.description.fil
Fil: de Prat Gay, Gonzalo. Fundación Instituto Leloir; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquimicas de Buenos Aires; Argentina
dc.journal.title
Protein Engineering Design & Selection
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/https://academic.oup.com/peds/article-lookup/doi/10.1093/protein/gzq064
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1093/protein/gzq064
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3003449/
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