title: Single molecule FRET for the study on structural dynamics of biomolecules.
abstract: Single molecule fluorescence resonance energy transfer (FRET) is the technique that has been developed by combining FRET measurement and single molecule fluorescence imaging. This technique allows us to measure the dynamic changes of the interaction and structures of biomolecules. In this study, the validity of the method was tested using fluorescence dyes on double stranded DNA molecules as a rigid spacer. FRET signals from double stranded DNA molecules were stable and their average FRET values provided the distance between the donor and acceptor in agreement with B-DNA type helix model. Next, the single molecule FRET method was applied to the studies on the dynamic structure of Ras, a signaling protein. The data showed that Ras has multiple conformational states and undergoes transition between them. This study on the dynamic conformation of Ras provided a clue for understanding the molecular mechanism of cell signaling switches.
authors.affiliation: Laboratories of Nanobiology, Graduate School of Frontier Biosciences, Osaka University 1-3, Yamadaoka, Suita, Osaka 565-0871, Japan.
authors.forename: Mitsuhiro
authors.initials: M
authors.lastname: Sugawa
authors.forename: Yoshiyuki
authors.initials: Y
authors.lastname: Arai
authors.forename: Atsuko Hikikoshi
authors.initials: AH
authors.lastname: Iwane
authors.forename: Yoshiharu
authors.initials: Y
authors.lastname: Ishii
authors.forename: Toshio
authors.initials: T
authors.lastname: Yanagida
mesh_terms: D004247:DNA / Q000737:chemistry; D031541:Fluorescence Resonance Energy Transfer / Q000295:instrumentation / Q000379:methods*; D005456:Fluorescent Dyes; D049490:Systems Biology; D013816:Thermodynamics; D018631:ras Proteins / Q000737:chemistry
chemical_list: D005456:Fluorescent Dyes; D004247:DNA; D018631:ras Proteins