Urea-induced denaturation of beta-trypsin: an evidence for a molten globule state.
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.
Brumano
Maria Helena Nasser
MH
Departamento de Bioquimica e Biologia Molecular, Universidade Federal de Vicosa, Vicosa, MG, 36571-000, Brazil.
Oliveira
Maria Goreti de Almeida
MG
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*
D000817:Anilino Naphthalenesulfonates; C035763:5,5'-bis(8-(phenylamino)-1-naphthalenesulfonate); D014508:Urea; D014357:Trypsin