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Biopolymers. 1991 Jan;31(1):119-28.

Study of the "molten globule" intermediate state in protein folding by a hydrophobic fluorescent probe.

Author information

1
Institute of Protein Research, Academy of Sciences of the USSR, Pushchino, Moscow Region.

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.

PMID:
2025683
DOI:
10.1002/bip.360310111
[Indexed for MEDLINE]

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