Journal
PROTEIN AND PEPTIDE LETTERS
Volume 11, Issue 2, Pages 133-140Publisher
BENTHAM SCIENCE PUBL LTD
DOI: 10.2174/0929866043478257
Keywords
beta-trypsin; urea denaturation; molten globule state
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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.
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