Photoacoustic spectroscopy of aromatic amino acids in proteins

dc.contributor.authorBugs, Milton Roque
dc.contributor.authorBortoleto-Bugs, Raquel Kely
dc.contributor.authorCornelio, Marinonio Lopes [UNESP]
dc.contributor.institutionCenPRA
dc.contributor.institutionCOGNITUS Project
dc.contributor.institutionUniversidade Estadual Paulista (Unesp)
dc.date.accessioned2014-05-20T14:02:35Z
dc.date.available2014-05-20T14:02:35Z
dc.date.issued2008-02-01
dc.description.abstractThis paper concerns the use of photoacoustic spectroscopy (PAS) to study the presence of aromatic amino acid in proteins. We examined the aromatic amino acids in six proteins with well-known structures using absorption spectra of near ultraviolet PAS over the wavelength range 240-320 nm. The fundamental understanding of the physical and chemical properties that govern the absorption of light and a subsequent release of heat to generate a transient pressure wave was used to test the concept of monitoring aromatic amino acids with this method. Second derivative spectroscopy in the ultraviolet region of proteins was also used to study the regions surrounding the aromatics and the percentage area in each band was related in order to determine the contribution in function of the respective molar extinction coefficients for each residue. Further investigation was conducted into the interaction between sodium dodecyl sulphate (SDS) and bothropstoxin-I (BthTx-I), with the purpose of identifying the aromatics that participate in the interaction. The clear changes in the second derivative and curve-fitting procedures suggest that initial SDS binding to the tryptophan located in the dimer interface and above 10 SDS an increased intensity between 260 and 320 nm, demonstrating that the more widespread tyrosine and phenylalanine residues contribute to the SDS/BthTx-I interactions. These results demonstrate the potential of near UV-PAS for the investigation of membrane proteins/detergent complexes in which light scattering is significant.en
dc.description.affiliationCenPRA, Ctr Pesquisas Renato Archer, BR-13069901 Campinas, SP, Brazil
dc.description.affiliationCOGNITUS Project, CENPES PETROBRAS, Rio de Janeiro, RJ, Brazil
dc.description.affiliationUNESP, IBILCE, Dept Fis, Sao Jose do Rio Preto, SP, Brazil
dc.description.affiliationUnespUNESP, IBILCE, Dept Fis, Sao Jose do Rio Preto, SP, Brazil
dc.format.extent205-212
dc.identifierhttp://dx.doi.org/10.1007/s00249-007-0217-4
dc.identifier.citationEuropean Biophysics Journal With Biophysics Letters. New York: Springer, v. 37, n. 2, p. 205-212, 2008.
dc.identifier.doi10.1007/s00249-007-0217-4
dc.identifier.issn0175-7571
dc.identifier.lattes3874425691257843
dc.identifier.urihttp://hdl.handle.net/11449/22061
dc.identifier.wosWOS:000252276700010
dc.language.isoeng
dc.publisherSpringer
dc.relation.ispartofEuropean Biophysics Journal With Biophysics Letters
dc.relation.ispartofjcr1.935
dc.relation.ispartofsjr0,604
dc.rights.accessRightsAcesso restrito
dc.sourceWeb of Science
dc.subjectPhotoacoustic spectroscopyen
dc.subjectaromatic amino acidsen
dc.subjectcurve-fittingen
dc.subjectbothropstoxin-Ien
dc.subjectSDSen
dc.titlePhotoacoustic spectroscopy of aromatic amino acids in proteinsen
dc.typeArtigo
dcterms.licensehttp://www.springer.com/open+access/authors+rights?SGWID=0-176704-12-683201-0
dcterms.rightsHolderSpringer
unesp.author.lattes3874425691257843
unesp.campusUniversidade Estadual Paulista (Unesp), Instituto de Biociências Letras e Ciências Exatas, São José do Rio Pretopt

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