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

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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.

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Biopolymers, v. 31, issue 1, p. 119-128