Study of the "molten globule" intermediate state in protein folding by a hydrophobic fluorescent probe - PubMed (original) (raw)
Study of the "molten globule" intermediate state in protein folding by a hydrophobic fluorescent probe
G V Semisotnov et al. Biopolymers. 1991 Jan.
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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