Abstract:
:The refolding kinetics of cobrotoxin (CBTX), a small-molecular-weight ( approximately 7 kDa) all beta-sheet protein, has been monitored using a variety of biophysical techniques. The secondary structure formation and hydrophobic collapse occur as distinct events during the refolding of the protein. Complete secondary structure formation occurs prior to the clustering of the hydrophobic residues. The late stage(s) of the refolding pathway of CBTX is characterized by change(s) in the local environment and optical asymmetry of the indole ring of the sole tryptophan residue. The results obtained in the present study, to our knowledge, represent the first unambiguous experimental support for the framework model of protein folding.
journal_name
Biochem Biophys Res Communjournal_title
Biochemical and biophysical research communicationsauthors
Sivaraman T,Kumar TK,Tu YT,Wang W,Lin WY,Chen HM,Yu Cdoi
10.1006/bbrc.1999.0901subject
Has Abstractpub_date
1999-06-24 00:00:00pages
284-8issue
1eissn
0006-291Xissn
1090-2104pii
S0006-291X(99)90901-4journal_volume
260pub_type
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