Literature DB >> 18958316

Time-resolved methods in biophysics. 8. Frequency domain fluorometry: applications to intrinsic protein fluorescence.

Justin A Ross1, David M Jameson.   

Abstract

Time-resolved fluorescence spectroscopy is an indispensable tool in the chemical, physical and biological sciences for the study of fast kinetic processes in the subpicosecond to microsecond time scale. This review focuses on the development and modern implementation of the frequency domain approach to time-resolved fluorescence. Both intensity decay (lifetime) and anisotropy decay (dynamic polarization) will be considered and their application to intrinsic protein fluorescence will be highlighted. In particular we shall discuss the photophysics of the aromatic amino acids, tryptophan, tyrosine and phenylalanine, which are responsible for intrinsic protein fluorescence. This discussion will be illustrated with examples of frequency domain studies on several protein systems.

Entities:  

Mesh：

Substances：

Year:  2008        PMID： 18958316     DOI： 10.1039/b804450n

Source DB:  PubMed          Journal:  Photochem Photobiol Sci        ISSN： 1474-905X            Impact factor:   3.982


  19 in total

Review 1.  Fluorescence polarization/anisotropy in diagnostics and imaging.

Authors:  David M Jameson; Justin A Ross
Journal:  Chem Rev       Date:  2010-05-12       Impact factor: 60.622

Review 2.  Fluorescence lifetime measurements and biological imaging.

Authors:  Mikhail Y Berezin; Samuel Achilefu
Journal:  Chem Rev       Date:  2010-05-12       Impact factor: 60.622

3.  Applications of phasors to in vitro time-resolved fluorescence measurements.

Authors:  Martin Stefl; Nicholas G James; Justin A Ross; David M Jameson
Journal:  Anal Biochem       Date:  2010-11-13       Impact factor: 3.365

4.  Applications of phasor plots to in vitro protein studies.

Authors:  Nicholas G James; Justin A Ross; Martin Stefl; David M Jameson
Journal:  Anal Biochem       Date:  2010-11-13       Impact factor: 3.365

5.  Dimeric endophilin A2 stimulates assembly and GTPase activity of dynamin 2.

Authors:  Justin A Ross; Yan Chen; Joachim Müller; Barbara Barylko; Lei Wang; Hunter B Banks; Joseph P Albanesi; David M Jameson
Journal:  Biophys J       Date:  2011-02-02       Impact factor: 4.033

Review 6.  Fluorescent analogs of biomolecular building blocks: design, properties, and applications.

Authors:  Renatus W Sinkeldam; Nicholas J Greco; Yitzhak Tor
Journal:  Chem Rev       Date:  2010-05-12       Impact factor: 60.622

7.  Ionic liquids increase the catalytic efficiency of a lipase (Lip1) from an antarctic thermophilic bacterium.

Authors:  Patricio A Muñoz; Daniela N Correa-Llantén; Jenny M Blamey
Journal:  Lipids       Date:  2014-11-27       Impact factor: 1.880

8.  Comparison of tryptophan fluorescence lifetimes in cyanobacterial photosystem I frozen in the light and in the dark.

Authors:  Peter P Knox; Boris N Korvatovskiy; Vladimir V Gorokhov; Sergey N Goryachev; Mahir D Mamedov; Vladimir Z Paschenko
Journal:  Photosynth Res       Date:  2018-10-23       Impact factor: 3.573

9.  Characterization of esterase activity from an Acetomicrobium hydrogeniformans enzyme with high structural stability in extreme conditions.

Authors:  Patricia S Kumagai; Raissa F Gutierrez; Jose L S Lopes; Julia M Martins; David M Jameson; Aline M Castro; Luiz F Martins; Ricardo DeMarco; Nelma R S Bossolan; B A Wallace; Ana P U Araujo
Journal:  Extremophiles       Date:  2018-07-16       Impact factor: 2.395

10.  Human serum transferrin: a tale of two lobes. Urea gel and steady state fluorescence analysis of recombinant transferrins as a function of pH, time, and the soluble portion of the transferrin receptor.

Authors:  Shaina L Byrne; Anne B Mason
Journal:  J Biol Inorg Chem       Date:  2009-03-17       Impact factor: 3.358
View more

北京卡尤迪生物科技股份有限公司 © 2022-2023.