Abstract:
:The cardiotoxin analogue III (CTX III), isolated from the Taiwan Cobra venom (Naja naja atra), is a sixty amino acid, all beta-sheet protein. The 2,2,2-trifluoro ethanol (TFE) induced unfolding of CTX III is studied under acidic conditions (pH 2.5). Using circular dichroism, 1-anilino-8-napthalene sulphonic acid binding and NMR experiments, it is shown that stable, partially structured state(s) ['molten globule'-like state] is formed between 50 and 80% TFE concentrations. The protein was found to exist in an unfolded state in 80% TFE containing 2M urea. The TFE induced unfolding process is shown to be completely reversible. In the 'molten globule' state of CTX III in 80% TFE, though portion(s) of the backbone of the protein assume helical conformation, most of the original beta-sheet secondary structural elements in the protein are intact. In our opinion, this is the first report of the identification of a 'molten globule'-like state in the unfolding pathway of an all beta-sheet monomeric protein.
journal_name
Biochem Biophys Res Communjournal_title
Biochemical and biophysical research communicationsauthors
Kumar TK,Jayaraman G,Lee CS,Sivaraman T,Lin WY,Yu Cdoi
10.1006/bbrc.1995.1221subject
Has Abstractpub_date
1995-02-15 00:00:00pages
536-43issue
2eissn
0006-291Xissn
1090-2104pii
S0006291X85712211journal_volume
207pub_type
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