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.
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
László
L
Mátyus
János
J
Szöllosi
Attila
A
Jenei
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