Single-molecule study of protein-protein and protein-DNA interaction dynamics.
Protein-protein and protein-DNA interactions play critical roles in biological systems, and these interactions often involve complex mechanisms and inhomogeneous dynamics. Single-molecule spectroscopy is a powerful and complimentary approach to decipher such spatially and temporally inhomogeneous protein interaction systems, providing new information that are not obtainable from static structure analyses, thermodynamics characterization, and ensemble-averaged measurements. To illustrate the single-molecule spectroscopy and imaging technology and their applications on studying protein-ligand interactions, this chapter focuses on discussing two recent single-molecule spectroscopy studies on protein-protein interaction in cell signaling process and on protein-DNA interactions in DNA damage recognition process.
Lu
H Peter
HP
Wiley Environmental Molecular Sciences Laboratory, Fundamental Science Division, Pacific Northwest National Laboratory, Richland, WA, USA.
D001665:Binding Sites; D015374:Biosensing Techniques; D004247:DNA / Q000737:chemistry* / Q000378:metabolism*; D004249:DNA Damage; D005454:Fluorescence Polarization; D031541:Fluorescence Resonance Energy Transfer; D006801:Humans; D066298:In Vitro Techniques; D008024:Ligands; D008280:Magnetics; D008958:Models, Molecular; D011485:Protein Binding; D011506:Proteins / Q000737:chemistry* / Q000378:metabolism*; D015398:Signal Transduction; D013050:Spectrometry, Fluorescence / Q000295:instrumentation / Q000379:methods*; D013816:Thermodynamics; D020764:cdc42 GTP-Binding Protein / Q000737:chemistry / Q000378:metabolism
D008024:Ligands; D011506:Proteins; D004247:DNA; D020764:cdc42 GTP-Binding Protein