You are in the accessibility menu

Please use this identifier to cite or link to this item: http://acervodigital.unesp.br/handle/11449/113192
Full metadata record
DC FieldValueLanguage
dc.contributor.authorBatista, Andrea N. L.-
dc.contributor.authorBatista, Joao M.-
dc.contributor.authorBolzani, Vanderlan da Silva-
dc.contributor.authorFurlan, Maysa-
dc.contributor.authorBlanch, Ewan W.-
dc.date.accessioned2014-12-03T13:11:28Z-
dc.date.accessioned2016-10-25T20:14:20Z-
dc.date.available2014-12-03T13:11:28Z-
dc.date.available2016-10-25T20:14:20Z-
dc.date.issued2013-01-01-
dc.identifierhttp://dx.doi.org/10.1039/c3cp53525h-
dc.identifier.citationPhysical Chemistry Chemical Physics. Cambridge: Royal Soc Chemistry, v. 15, n. 46, p. 20147-20152, 2013.-
dc.identifier.issn1463-9076-
dc.identifier.urihttp://hdl.handle.net/11449/113192-
dc.identifier.urihttp://acervodigital.unesp.br/handle/11449/113192-
dc.description.abstractThe function of a protein is determined by its structure, which is intrinsically related to its solvent environment. Based on this paradigm, there has been a great deal of interest in the role that nonaqueous solvents play in regulating protein structure, with some debate in the literature regarding dimethyl sulfoxide (DMSO). Thus, in this work we have used Raman and Raman optical activity (ROA) spectroscopies to investigate conclusively the changes induced by DMSO in the secondary structure of an array of proteins including human serum albumin (highly alpha-helical), bovine alpha-lactalbumin (mainly alpha-helical), bovine ribonuclease A (containing both alpha-helix and beta-sheet), bovine beta-lactoglobulin (mainly beta-sheet), and bovine alpha-casein (disordered). Our results clearly demonstrate that 100% DMSO solutions destabilize alpha-helices completely, converting them into the poly(L-proline) II (PPII) helix conformation. However, low concentrations of DMSO (10% v/v) were found to have little effect on the structure of even the most helical protein, human serum albumin. In the case of alpha-casein, the natively unfolded protein rich in PPII helix was converted into a further disordered structure when dissolved in pure DMSO. By contrast, beta-sheets remained mostly unaffected regardless of DMSO concentration. While providing new insights into protein structure in organic solvents, this work reinforces the capability of vibrational optical activity to assess conformations of biomolecules in conditions not accessible to other techniques, such as X-ray crystallography and NMR.en
dc.description.sponsorshipManchester Chemical Biology Network (MCBN)-
dc.description.sponsorshipFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)-
dc.description.sponsorshipConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)-
dc.format.extent20147-20152-
dc.language.isoeng-
dc.publisherRoyal Soc Chemistry-
dc.sourceWeb of Science-
dc.titleSelective DMSO-induced conformational changes in proteins from Raman optical activityen
dc.typeoutro-
dc.contributor.institutionUniversity of Manchester-
dc.contributor.institutionUniversidade Estadual Paulista (UNESP)-
dc.description.affiliationUniv Manchester, Manchester Inst Biotechnol, Manchester M1 7DN, Lancs, England-
dc.description.affiliationUniv Manchester, Fac Life Sci, Manchester M1 7DN, Lancs, England-
dc.description.affiliationUniv Estadual Paulista UNESP, Dept Quim Organ, BR-14800900 Araraquara, Brazil-
dc.description.affiliationUnespUniv Estadual Paulista UNESP, Dept Quim Organ, BR-14800900 Araraquara, Brazil-
dc.description.sponsorshipIdFAPESP: 13/07600-3-
dc.description.sponsorshipIdFAPESP: 11/01003-4-
dc.description.sponsorshipIdFAPESP: 12/16484-4-
dc.description.sponsorshipIdFAPESP: 11/22339-4-
dc.description.sponsorshipIdFAPESP: 12/13739-1-
dc.identifier.doi10.1039/c3cp53525h-
dc.identifier.wosWOS:000326747200023-
dc.rights.accessRightsAcesso restrito-
dc.relation.ispartofPhysical Chemistry Chemical Physics-
Appears in Collections:Artigos, TCCs, Teses e Dissertações da Unesp

There are no files associated with this item.
 

Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.