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