Determination of structural and thermodynamic parameters of bovine α- trypsin isoform in aqueous-organic media

Página do item simplificado
dc.creatorDayanne Pinho Rosa
dc.creatorAlexandre Martins Costa Santos
dc.creatorEvaldo Vitor Pereira
dc.creatorAntonio Victor Baioco Vasconcelos
dc.creatorMaria Aparecida Cicilini
dc.creatorAndré Romero da Silva
dc.creatorCaroline Dutra Lacerda
dc.creatorJamil Silvano de Oliveira
dc.creatorMarcelo Matos Santoro
dc.creatorJuliana Barbosa Coitinho
dc.date.accessioned2022-02-18T21:36:40Z
dc.date.accessioned2025-09-09T00:28:07Z
dc.date.available2022-02-18T21:36:40Z
dc.date.issued2017-08
dc.identifier.doi10.1016/j.ijbiomac.2017.03.125
dc.identifier.issn01418130
dc.identifier.urihttps://hdl.handle.net/1843/39483
dc.languageeng
dc.publisherUniversidade Federal de Minas Gerais
dc.relation.ispartofInternational journal of biological macromolecules
dc.rightsAcesso Restrito
dc.subjectBiofísica
dc.subject.otherα-trypsin
dc.subject.otherisoforms
dc.subject.otherorganic solvent
dc.subject.otherthermodynamic
dc.titleDetermination of structural and thermodynamic parameters of bovine α- trypsin isoform in aqueous-organic media
dc.title.alternativeDeterminação de parâmetros estruturais e termodinâmicos da isoforma de α-tripsina bovina em meio aquoso-orgânico
dc.typeArtigo de periódico
local.citation.epage416
local.citation.spage408
local.citation.volume101
local.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.
local.publisher.countryBrasil
local.publisher.departmentICB - INSTITUTO DE CIÊNCIAS BIOLOGICAS
local.publisher.initialsUFMG
local.url.externahttps://www.sciencedirect.com/science/article/abs/pii/S0141813017300144?via%3Dihub

Arquivos

Licença do pacote

Agora exibindo 1 - 1 de 1
Imagem de Miniatura
Nome:
License.txt
Tamanho:
1.99 KB
Formato:
Plain Text
Descrição:
Baixar

Coleções

Artigo de Periódico

Logo UFMG