title: Study of the "molten globule" intermediate state in protein folding by a hydrophobic fluorescent probe.
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.
authors.affiliation: Institute of Protein Research, Academy of Sciences of the USSR, Pushchino, Moscow Region.
authors.forename: G V
authors.initials: GV
authors.lastname: Semisotnov
authors.forename: N A
authors.initials: NA
authors.lastname: Rodionova
authors.forename: O I
authors.initials: OI
authors.lastname: Razgulyaev
authors.forename: V N
authors.initials: VN
authors.lastname: Uversky
authors.forename: A F
authors.initials: AF
authors.lastname: Gripas'
authors.forename: R I
authors.initials: RI
authors.lastname: Gilmanshin
mesh_terms: D000817:Anilino Naphthalenesulfonates; D000818:Animals; D005456:Fluorescent Dyes; D006801:Humans; D007700:Kinetics; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry*
chemical_list: D000817:Anilino Naphthalenesulfonates; D005456:Fluorescent Dyes; D011506:Proteins; C027132:1-anilino-8-naphthalenesulfonate