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Thermal denaturation of an all beta-sheet protein--identification of a stable partially structured intermediate at
G Jayaraman1, T K Kumar, T Sivaraman
1Department of Chemistry, National Tsing Hua University, Hsinchu, Taiwan, Republic of China.
International Journal of Biological Macromolecules
|June 1, 1996
Abstract:
The thermal unfolding of an all beta-sheet protein, cardiotoxin analogue III, from the Taiwan Cobra (Naja naja atra) is studied at pH 2.0, 4.0 and 6.0. At pH 4.0, using circular dichroism and 1-anilino naphthalene-8-sulphonic acid (ANS) fluorescence binding studies, a stable partially structured intermediate is detected at 90 degrees C.