Probing single-molecule protein conformational dynamics.
Protein conformational fluctuations and dynamics, often complex and associated with inhomogeneities, play a crucial role in biomolecular functions. It is extremely difficult to characterize such inhomogeneous dynamics in an ensemble-averaged measurement, especially when the proteins are involved in multiple-step, multiple-conformation complex chemical interactions and transformations, such as in enzymatic reactions, protein-protein interactions, and ion-channel membrane protein processes. Alternatively, single-molecule spectroscopy is a powerful approach to probing and analyzing protein conformational dynamics in real time.
Lu
H Peter
HP
Pacific Northwest National Laboratory, Fundamental Science Division, P.O. Box 999, Richland, Washington 99352, USA. peter.lu@pnl.gov
D017122:Bacteriophage T4 / Q000201:enzymology; D019281:Dimerization; D031541:Fluorescence Resonance Energy Transfer; D006096:Gramicidin / Q000737:chemistry*; D007473:Ion Channels / Q000737:chemistry; D008051:Lipid Bilayers / Q000737:chemistry; D008565:Membrane Proteins / Q000737:chemistry; D009113:Muramidase / Q000737:chemistry*; D011487:Protein Conformation; D015398:Signal Transduction; D013050:Spectrometry, Fluorescence / Q000379:methods*; D014764:Viral Proteins / Q000737:chemistry; D020764:cdc42 GTP-Binding Protein / Q000737:chemistry* / Q000378:metabolism
D007473:Ion Channels; D008051:Lipid Bilayers; D008565:Membrane Proteins; D014764:Viral Proteins; D006096:Gramicidin; D009113:Muramidase; D020764:cdc42 GTP-Binding Protein