Study of the "molten globule" intermediate state in protein folding by a hydrophobic fluorescent probe.
作者： G. V. Semisotnov , N. A. Rodionova , O. I. Razgulyaev , V. N. Uversky , A. F. Gripas'
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摘要: 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 shown that ANS much stronger affinity protein "molten globule" state, pronounced secondary structure compactness, but without tightly packed tertiary as compared its native coil-like proteins, or coil-like, alpha-helical, beta-structural hydrophilic homopolypeptides. The possibility using for study equilibrium kinetic molten globule intermediates is demonstrated, carbonic anhydrase, beta-lactamase, alpha-lactalbumin examples.
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