Visualizing and manipulating individual protein molecules.
Single-molecule imaging and manipulation techniques have evolved in the past decade from mere jaw-dropping attractions to essential laboratory tools. By applying single-molecule methods important insights otherwise unavailable have been obtained on various biomolecular systems. Constantly improving single-molecule imaging techniques keep expanding the scale of the explorable spatial detail, thereby providing possible solutions to getting around the debilitating diffraction limit present in physiological-condition structural investigations. In some areas, such as motor protein studies, single-molecule methods have become part of the routine and essential research toolkit. Entire research fields, such as single-molecule force spectroscopy, have been born. In the present review single-molecule visualization and manipulation methods are reviewed with a focus on proteins. Relevant signals and prominent applications are discussed along with experimental examples and recent important results. Finally, the perspectives of the single-molecule field are explored.
Kellermayer
Miklós S Z
MS
Department of Biophysics, Faculty of Medicine, University of Pécs, Szigeti út 12. Pécs H-7624, Hungary. Miklos.Kellermayer.Jr@aok.pte.hu
D004548:Elasticity; D007090:Image Interpretation, Computer-Assisted / Q000379:methods*; D008846:Micromanipulation / Q000379:methods*; D018625:Microscopy, Atomic Force / Q000379:methods*; D008856:Microscopy, Fluorescence / Q000379:methods*; D008967:Molecular Biology / Q000379:methods; D011487:Protein Conformation; D011506:Proteins / Q000032:analysis / Q000737:chemistry* / Q000648:ultrastructure*; D013314:Stress, Mechanical
D011506:Proteins