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

✍ Scribed by G. V. Semisotnov; N. A. Rodionova; O. I. Razgulyaev; V. N. Uversky; A. F. Gripas'; R. I. Gilmanshin

Publisher
Wiley (John Wiley & Sons)
Year
1991
Tongue
English
Weight
772 KB
Volume
31
Category
Article
ISSN
0006-3525

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✦ Synopsis

of Sciences of the USSR, 142292 Pushchino, Moscow Region, USSR

SYNOPSIS

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, a-helical, or p-structural hydrophilic homopolypeptides.

The possibility of using ANS for the study of equilibrium and kinetic molten globule intermediates is demonstrated, with carbonic anhydrase, p-lactamase, and a-lactalbumin as examples.

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