Identification of folding intermediates of streblin, the most stable serine protease: biophysical analysis

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MetadadosDescriçãoIdioma
Autor(es): dc.contributorUniversidade Estadual Paulista (UNESP)-
Autor(es): dc.creatorKumar, Reetesh-
Autor(es): dc.creatorTripathi, Pinki-
Autor(es): dc.creatorMoraes, Fabio Rogerio de-
Autor(es): dc.creatorCaruso, Icaro P.-
Autor(es): dc.creatorJagannadham, Medicherla V.-
Data de aceite: dc.date.accessioned2021-03-10T21:17:33Z-
Data de disponibilização: dc.date.available2021-03-10T21:17:33Z-
Data de envio: dc.date.issued2014-12-03-
Data de envio: dc.date.issued2014-12-03-
Data de envio: dc.date.issued2014-01-01-
Fonte completa do material: dc.identifierhttp://dx.doi.org/10.1007/s12010-013-0565-8-
Fonte completa do material: dc.identifierhttp://hdl.handle.net/11449/111573-
Fonte: dc.identifier.urihttp://educapes.capes.gov.br/handle/11449/111573-
Descrição: dc.descriptionCSIR/CSIR-
Descrição: dc.descriptionDBT-
Descrição: dc.descriptionUGC, Government of India-
Descrição: dc.descriptionStreblin, a serine proteinase from plant Streblus asper, has been used to investigate the conformational changes induced by pH, temperature, and chaotropes. The near/far UV circular dichroism activities under fluorescence emission spectroscopy and 8-aniline-1-naphthalene sulfonate (ANS) binding have been carried out to understand the unfolding of the protein in the presence of denaturants. Spectroscopic studies reveal that streblin belongs to the alpha+beta class of proteins and exhibits stability towards chemical denaturants, guanidine hydrochloride (GuHCl). The pH-induced transition of this protein is noncooperative for transition phases between pH 0.5 and 2.5 (midpoint, 1.5) and pH 2.5 and 10.0 (midpoint, 6.5). At pH 1.0 or lower, the protein unfolds to form acid-unfolded state, and for pH 7.5 and above, protein turns into an alkaline denatured state characterized by the absence of ANS binding. At pH 2.0 (1M GuHCl), streblin exists in a partially unfolded state with characteristics of amolten globule state. The protein is found to exhibit strong and predominant ANS binding. In total, six different intermediate states has been identified to show protein folding pathways.-
Formato: dc.format658-671-
Idioma: dc.languageen-
Publicador: dc.publisherHumana Press Inc-
Relação: dc.relationApplied Biochemistry and Biotechnology-
Relação: dc.relation1.797-
Relação: dc.relation0,571-
Direitos: dc.rightsopenAccess-
Palavras-chave: dc.subjectSequential unfolding-
Palavras-chave: dc.subjectStreblin-
Palavras-chave: dc.subjectStreblus asper-
Palavras-chave: dc.subjectBiophysics-
Palavras-chave: dc.subjectMolten globule-
Título: dc.titleIdentification of folding intermediates of streblin, the most stable serine protease: biophysical analysis-
Tipo de arquivo: dc.typelivro digital-
Aparece nas coleções:Repositório Institucional - Unesp

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