title: Urea-induced denaturation of beta-trypsin: an evidence for a molten globule state.
abstract: The denaturation of beta-trypsin induced by urea was investigated by fluorescence and circular dichroism. A transient denatured state was found at 2 M urea in both intrinsic fluorescence spectrum and bis-(8-anilino-1-naphtalene sulfonate) (bis-ANS) binding. In addition, the absence of tertiary contacts and presence of secondary structure for this state, are consistent with an intermediate equilibrium state having features of molten globule.
authors.affiliation: Departamento de Bioquimica e Biologia Molecular, Universidade Federal de Vicosa, Vicosa, MG, 36571-000, Brazil.
authors.forename: Maria Helena Nasser
authors.initials: MH
authors.lastname: Brumano
authors.forename: Maria Goreti de Almeida
authors.initials: MG
authors.lastname: Oliveira
mesh_terms: D000817:Anilino Naphthalenesulfonates / Q000737:chemistry; D000818:Animals; D002417:Cattle; D002942:Circular Dichroism; D004795:Enzyme Stability; D006863:Hydrogen-Ion Concentration; D011489:Protein Denaturation; D017510:Protein Folding; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D013050:Spectrometry, Fluorescence; D014357:Trypsin / Q000737:chemistry*; D014508:Urea / Q000737:chemistry*
chemical_list: D000817:Anilino Naphthalenesulfonates; C035763:5,5'-bis(8-(phenylamino)-1-naphthalenesulfonate); D014508:Urea; D014357:Trypsin