The study of protein folding and dynamics by determination of intramolecular distance distributions and their fluctuations using ensemble and single-molecule FRET measurements.
The folding and dynamics of globular proteins is a multidimensional problem. The structures of the heterogeneous population of refolding protein molecules are characterized by multiple distances and time constants. Deciphering the mechanism of folding depends on studies of the processes rather than the folded structures alone. Spectroscopy is indispensable for these sorts of studies. Herein, it is shown that the determination of intramolecular distance distributions by ensemble and single-molecule FRET experiments enable the exploration of partially folded states of refolding protein molecules.
Haas
Elisha
E
Faculty of Life Sciences, Bar Ilan University, Ramat Gan 52900, Israel. haas@mail.biu.ac.il
D000263:Adenylate Kinase / Q000737:chemistry; D000818:Animals; D007611:Aprotinin / Q000737:chemistry; D001703:Biophysics / Q000379:methods; D002417:Cattle; D003432:Cross-Linking Reagents / Q000494:pharmacology; D004735:Energy Transfer; D004926:Escherichia coli / Q000378:metabolism; D031541:Fluorescence Resonance Energy Transfer / Q000379:methods*; D007700:Kinetics; D008958:Models, Molecular; D015233:Models, Statistical; D008968:Molecular Conformation; D009154:Mutation; D011487:Protein Conformation; D011489:Protein Denaturation; D017510:Protein Folding; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D011506:Proteins / Q000737:chemistry*; D013269:Stochastic Processes; D013997:Time Factors
D003432:Cross-Linking Reagents; D011506:Proteins; D007611:Aprotinin; D000263:Adenylate Kinase