Study of the “molten globule” intermediate state in protein folding by a hydrophobic fluorescent probe

1991/01/01 by G. V. Semisotnov, Gennady V. Semisotnov, N. A. Rodionova +9 · 27 citations
Biochemistry, Genetics and Molecular Biology · Materials Science · #Protein Structure and Dynamics #Enzyme Structure and Function #Hemoglobin structure and function

paper · doi:10.1002/bip.360310111

Abstract

Binding of the hydrophobic 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, alpha-helical, or beta-structural hydrophilic homopolypeptides. The possibility of using ANS for the study of equilibrium and kinetic molten globule intermediates is demonstrated, with carbonic anhydrase, beta-lactamase, and alpha-lactalbumin as examples.

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