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Please use this identifier to cite or link to this item: http://hdl.handle.net/1843/39483
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dc.creatorDayanne Pinho Rosapt_BR
dc.creatorAlexandre Martins Costa Santospt_BR
dc.creatorEvaldo Vitor Pereirapt_BR
dc.creatorAntonio Victor Baioco Vasconcelospt_BR
dc.creatorMaria Aparecida Cicilinipt_BR
dc.creatorAndré Romero da Silvapt_BR
dc.creatorCaroline Dutra Lacerdapt_BR
dc.creatorJamil Silvano de Oliveirapt_BR
dc.creatorMarcelo Matos Santoropt_BR
dc.creatorJuliana Barbosa Coitinhopt_BR
dc.date.accessioned2022-02-18T21:36:40Z-
dc.date.available2022-02-18T21:36:40Z-
dc.date.issued2017-08-
dc.citation.volume101pt_BR
dc.citation.spage408pt_BR
dc.citation.epage416pt_BR
dc.identifier.doi10.1016/j.ijbiomac.2017.03.125pt_BR
dc.identifier.issn01418130pt_BR
dc.identifier.urihttp://hdl.handle.net/1843/39483-
dc.description.resumoThe α-trypsin isoform is a globular protein that belongs to serine-protease family and has a polypeptide chain of 223 amino acid residues, six disulfide bridges and two domains with similar structures. The effects of aqueous-organic solvent (ethanol) in different concentration on the α-trypsin structure have been investigated by spectroscopic techniques and thermodynamic data analysis. The results from spectroscopic measurements, including far-UV Circular Dichroism, UV–vis absorption spectroscopy, intrinsic tryptophan fluorescence and dynamic light scattering (DLS) suggest the formation of partially folded states, instead of aggregate states, at high ethanol concentration (>60% v/v ethanol), with little loss of secondary structure, but with significant tertiary structure changes. The thermodynamic data (Tm and ΔH) suggest a loosening of intramolecular weak interactions, which reflects in a flexibility increase such that the catalytic capacity can be increased or decreased according to the ethanol concentration into the system. Overall results we suggest that in range of 0–60% v/v ethanol/buffer, α-trypsin undergoes reversible multimerization phenomena with catalytic activity. However from 60% v/v ethanol/buffer, population of folded partially states with less catalytic activity are predominant.pt_BR
dc.languageengpt_BR
dc.publisherUniversidade Federal de Minas Geraispt_BR
dc.publisher.countryBrasilpt_BR
dc.publisher.departmentICB - INSTITUTO DE CIÊNCIAS BIOLOGICASpt_BR
dc.publisher.initialsUFMGpt_BR
dc.relation.ispartofInternational journal of biological macromoleculespt_BR
dc.rightsAcesso Restritopt_BR
dc.subjectα-trypsinpt_BR
dc.subjectisoformspt_BR
dc.subjectorganic solventpt_BR
dc.subjectthermodynamicpt_BR
dc.subject.otherBiofísicapt_BR
dc.titleDetermination of structural and thermodynamic parameters of bovine α- trypsin isoform in aqueous-organic mediapt_BR
dc.title.alternativeDeterminação de parâmetros estruturais e termodinâmicos da isoforma de α-tripsina bovina em meio aquoso-orgânicopt_BR
dc.typeArtigo de Periódicopt_BR
dc.url.externahttps://www.sciencedirect.com/science/article/abs/pii/S0141813017300144?via%3Dihubpt_BR
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