Steady-state fluorescence quenching applications for studying protein structure and dynamics.
Fluorescence quenching methods are useful to obtain information about the conformational and/or dynamic changes of proteins in complex macromolecular systems. In this review steady-state methods are described and the data interpretation is thoroughly discussed. As a special case of fluorescence quenching mechanism, fluorescence resonance energy transfer (FRET) phenomenon is also presented. Application of a FRET based method to characterize the temperature dependence of the flexibility of protein matrix is clearly demonstrated.
Mátyus
László
L
Department of Biophysics and Cell Biology, Research Center for Molecular Medicine, Medical and Health Science Center, University of Debrecen, Nagyerdei krt 98, P.O. Box 39, H-4012 Debrecen, Hungary. lmatyus@jaguar.dote.hu
Szöllosi
János
J
Jenei
Attila
A
D020106:Acrylamide / Q000737:chemistry; D000465:Algorithms; D002586:Cesium / Q000737:chemistry; D002712:Chlorides / Q000737:chemistry; D004735:Energy Transfer; D005453:Fluorescence; D031541:Fluorescence Resonance Energy Transfer / Q000379:methods*; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry* / Q000378:metabolism; D013696:Temperature; D014364:Tryptophan / Q000737:chemistry*
D002712:Chlorides; D011506:Proteins; D002586:Cesium; D020106:Acrylamide; D014364:Tryptophan; C028019:cesium chloride