Study of the “Molten Globule” Intermediate State in Protein Folding by a Hydrophobic Fluorescent Probe
Digital Object Identifier (DOI)
Binding of the hydrophobia fluorescent probe, 1-anilino-naphthalene-8-sulfonate (ANS), to synthetic polypeptides and proteins with a different structural organization has been studied. It has been shown that ANS has a much stronger affinity to the protein “molten globule” state, with a pronounced secondary structure and compactness, but without a tightly packed tertiary structure as compared with its affinity to the native and coil-like proteins, or to coil-like, α-helical, or β-structural hydrophilic homopolypeptides.
The possibility of using ANS for the study of equilibrium and kinetic molten globule intermediates is demonstrated, with carbonic anhydrase, β-lactamase, and α-lactalbumin as examples.
Was this content written or created while at USF?
Citation / Publisher Attribution
Biopolymers, v. 31, issue 1, p. 119-128
Scholar Commons Citation
Semisotnov, G. V.; Rodionova, N. A.; Razgulyaev, O. I.; Uversky, Vladimir N.; Gripas, A. F.; and I. Gilmanshin, R., "Study of the “Molten Globule” Intermediate State in Protein Folding by a Hydrophobic Fluorescent Probe" (1991). Molecular Medicine Faculty Publications. 619.