[ANS fluorescence. II. Use of the method of fluorescent probe decay for studying the structural transformations in globular proteins].
Changes in ANS fluorescence decay parameters induced by the interaction of the probe with proteins have been investigated. The existence of at least two different modes of interactions between the ANS and protein was established. The interactions of the first type are connected with binding of an ANS molecule with the surface of a protein molecule. In this case ANS molecules are well acceptable for a solvent. The interactions of the second type are characteristic of the protein-embedded ANS molecules. The decay time values of the second type complexes change considerably (> 1.5-fold) during the protein molecule transformation into the molten globule-like conformation. The molecular model explaining such a behaviour is suggested.
Uverskiĭ
V N
VN
Institute for Biological Instrumentation, Russian Academy of Sciences, Pushchino.
D000817:Anilino Naphthalenesulfonates / Q000737:chemistry*; D005456:Fluorescent Dyes; D008958:Models, Molecular; D015394:Molecular Structure; D011487:Protein Conformation; D012995:Solubility; D013499:Surface Properties
D000817:Anilino Naphthalenesulfonates; D005456:Fluorescent Dyes; C027132:1-anilino-8-naphthalenesulfonate
Fluorestsentsiia ANS. II. Primenenie metoda zatukhaniia fluorestsentsii zonda dlia issledovaniia strukturnykh prevrashcheniĭ v globuliarnykh belkakh.