Study of the “Molten Globule” Intermediate State in Protein Folding by a Hydrophobic Fluorescent Probe

Authors

G. V. Semisotnov, Institute of Protein Research of the Russian Academy of Sciences
N. A. Rodionova, Institute of Protein Research of the Academy of Sciences
O. I. Razgulyaev, Institute of Protein Research of the Academy of Sciences
Vladimir N. Uversky, Academy of Sciences of the USSRFollow
A. F. Gripas, Institute of Protein Research of the Academy of Sciences
R. I. Gilmanshin, Institute of Protein Research of the Academy of Sciences

Document Type

Article

Publication Date

1991

Digital Object Identifier (DOI)

https://doi.org/10.1002/bip.360310111

Abstract

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?

Yes

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.
https://digitalcommons.usf.edu/mme_facpub/619