title: Secondary structure formation is the earliest structural event in the refolding of an all beta-sheet protein.
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.
authors.affiliation: Department of Chemistry, National Tsing Hua University, Hsinchu, Taiwan, 30043, Republic of China.
authors.forename: T
authors.initials: T
authors.lastname: Sivaraman
authors.forename: T K
authors.initials: TK
authors.lastname: Kumar
authors.forename: Y T
authors.initials: YT
authors.lastname: Tu
authors.forename: W
authors.initials: W
authors.lastname: Wang
authors.forename: W Y
authors.initials: WY
authors.lastname: Lin
authors.forename: H M
authors.initials: HM
authors.lastname: Chen
authors.forename: C
authors.initials: C
authors.lastname: Yu
mesh_terms: D003039:Cobra Neurotoxin Proteins / Q000737:chemistry*; D007700:Kinetics; D009682:Magnetic Resonance Spectroscopy; D008958:Models, Molecular; D017510:Protein Folding; D017433:Protein Structure, Secondary; D013997:Time Factors
chemical_list: D003039:Cobra Neurotoxin Proteins