Unfolding processes of small globular proteins: the two-state vs multi-state model.
1. The alcohol-induced unfolding of two homologous proteins, neurotoxin and cardiotoxin from Taiwan cobra (Naja naja atra) venom has been analysed. 2. It is postulated that the unfolding process for both proteins is a multi-state conformational transition. 3. It has been hypothesized that between the compact native state of the protein and its fully unfolded state there exists a quasi-continuous spectrum of conformational metastates of protein species. 4. The population distribution of these metastates is partially dependent on the nature of unfolding factors as well as the amino acid composition and sequence. 5. The sum of all transient conformational states and the protein species being in the folded and unfolded states respectively, can be detected by means of circular dichroism spectroscopy since the absorption of circularly polarized light is rapid relative to the rate of fluctuations of the protein structure.
D000818:Animals; D055598:Chemical Phenomena; D002621:Chemistry; D004179:Cobra Cardiotoxin Proteins / Q000302:isolation & purification*; D003039:Cobra Neurotoxin Proteins / Q000302:isolation & purification*; D004546:Elapid Venoms / Q000032:analysis / Q000302:isolation & purification*; D008956:Models, Chemical; D011487:Protein Conformation
D004179:Cobra Cardiotoxin Proteins; D003039:Cobra Neurotoxin Proteins; D004546:Elapid Venoms