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Urea-Induced Denaturation of β-Trypsin: An Evidence for a Molten Globule State

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The denaturation of β-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.

Keywords: molten globule state; trypsin; urea denaturation

Document Type: Review Article


Affiliations: Departamento de Bioquimica e Biologia Molecular, Universidade Federal de Vicosa, Vicosa, MG, 36571-000, Brazil.

Publication date: April 1, 2004

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  • Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.

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