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dc.contributor.CRUESPUNIVERSIDADE ESTADUAL DE CAMPINASpt_BR
dc.contributor.authorunicampNorberto, Douglas Ricardo-
dc.typeArtigopt_BR
dc.titleCavities determine the pressure unfolding of proteinspt_BR
dc.contributor.authorRoche, Julien-
dc.contributor.authorCaro, Jose A.-
dc.contributor.authorNorberto, Douglas R.-
dc.contributor.authorBarthe, Philippe-
dc.contributor.authorRoumestand, Christian-
dc.contributor.authorSchlessman, Jamie L.-
dc.contributor.authorGarcia, Angel E.-
dc.contributor.authorGarcia-Moreno E, Bertrand-
dc.contributor.authorRoyer, Catherine A.-
dc.subjectCavidadespt_BR
dc.subject.otherlanguageCavitiespt_BR
dc.description.abstractIt has been known for nearly 100 years that pressure unfolds proteins, yet the physical basis of this effect is not understood. Unfolding by pressure implies that the molar volume of the unfolded state of a protein is smaller than that of the folded state. This decrease in volume has been proposed to arise from differences between the density of bulk water and water associated with the protein, from pressure-dependent changes in the structure of bulk water, from the loss of internal cavities in the folded states of proteins, or from some combination of these three factors. Here, using 10 cavity-containing variants of staphylococcal nuclease, we demonstrate that pressure unfolds proteins primarily as a result of cavities that are present in the folded state and absent in the unfolded one. High-pressure NMR spectroscopy and simulations constrained by the NMR data were used to describe structural and energetic details of the folding landscape of staphylococcal nuclease that are usually inaccessible with existing experimental approaches using harsher denaturants. Besides solving a 100-year-old conundrum concerning the detailed structural origins of pressure unfolding of proteins, these studies illustrate the promise of pressure perturbation as a unique tool for examining the roles of packing, conformational fluctuations, and water penetration as determinants of solution properties of proteins, and for detecting folding intermediates and other structural details of protein-folding landscapes that are invisible to standard experimental approachespt_BR
dc.relation.ispartofProceedings of the National Academy of Sciences of the United States of Americapt_BR
dc.relation.ispartofabbreviationProc. Natl. Acad. Sci. U. S. A.pt_BR
dc.publisher.cityWashington, DCpt_BR
dc.publisher.countryEstados Unidospt_BR
dc.publisherNational Academy of Sciencespt_BR
dc.date.issued2012-
dc.date.monthofcirculationMaypt_BR
dc.language.isoengpt_BR
dc.description.volume109pt_BR
dc.description.issuenumber18pt_BR
dc.description.firstpage6945pt_BR
dc.description.lastpage6950pt_BR
dc.rightsFechadopt_BR
dc.sourceWOSpt_BR
dc.identifier.issn0027-8424pt_BR
dc.identifier.eissn1091-6490pt_BR
dc.identifier.doi10.1073/pnas.1200915109pt_BR
dc.identifier.urlhttps://www.pnas.org/content/109/18/6945pt_BR
dc.description.sponsorshipCOORDENAÇÃO DE APERFEIÇOAMENTO DE PESSOAL DE NÍVEL SUPERIOR - CAPESpt_BR
dc.description.sponsordocumentnumbersem informaçãopt_BR
dc.date.available2020-09-01T12:49:07Z-
dc.date.accessioned2020-09-01T12:49:07Z-
dc.description.provenanceSubmitted by Sanches Olivia (olivias@unicamp.br) on 2020-09-01T12:49:07Z No. of bitstreams: 0. Added 1 bitstream(s) on 2021-01-04T15:14:48Z : No. of bitstreams: 1 000303602100042.pdf: 2128514 bytes, checksum: 82d369dea3d978320b4b340d07711ca0 (MD5)en
dc.description.provenanceMade available in DSpace on 2020-09-01T12:49:07Z (GMT). No. of bitstreams: 0 Previous issue date: 2012en
dc.identifier.urihttp://repositorio.unicamp.br/jspui/handle/REPOSIP/348420-
dc.contributor.departmentsem informaçãopt_BR
dc.contributor.unidadeInstituto de Biologiapt_BR
dc.subject.keywordEnergy landscapept_BR
dc.subject.keywordFluorescencept_BR
dc.subject.keywordVolume changept_BR
dc.identifier.source000303602100042pt_BR
dc.creator.orcid0000-0002-2649-4251pt_BR
dc.type.formArtigo de pesquisapt_BR
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