Thermal denaturation of an all beta-sheet protein--identification of a stable partially structured intermediate at high temperature.
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.
Jayaraman
G
G
Department of Chemistry, National Tsing Hua University, Hsinchu, Taiwan, Republic of China.
Kumar
T K
TK
Sivaraman
T
T
Lin
W Y
WY
Chang
D K
DK
Yu
C
C
D000817:Anilino Naphthalenesulfonates; D000818:Animals; D002942:Circular Dichroism; D004179:Cobra Cardiotoxin Proteins / Q000737:chemistry*; D004355:Drug Stability; D005456:Fluorescent Dyes; D006358:Hot Temperature; D006863:Hydrogen-Ion Concentration; D046911:Macromolecular Substances; D015394:Molecular Structure; D011489:Protein Denaturation; D017433:Protein Structure, Secondary; D013050:Spectrometry, Fluorescence
D000817:Anilino Naphthalenesulfonates; D004179:Cobra Cardiotoxin Proteins; D005456:Fluorescent Dyes; D046911:Macromolecular Substances; C082202:cardiotoxin III, Naja naja atra