Single-molecule imaging by atomic force microscopy of the native chaperonin complex of the thermophilic archaeon Sulfolobus solfataricus.
The chaperonin of the extremely thermophilic archaeon Sulfolobus solfataricus has been imaged for the first time under native conditions using the atomic force microscope. This technique allows to visualize the structure of biomolecules in solution under physiological conditions providing a nanometer resolution topographic image of the sample. Single molecule studies can reveal fine structural details, providing a powerful insight into the active conformation of a macromolecule, and also allowing to detect different conformational states corresponding to functional changes.
Valle
F
F
Institut de Physique de la Matière Condensée, Université de Lausanne, BSP, CH-1015 Lausanne-Dorigny, Switzerland. francesco.valle@ipmc.unil.ch
Dietler
G
G
Londei
P
P
D019843:Archaeal Proteins; D018833:Chaperonins / Q000737:chemistry / Q000648:ultrastructure; D006360:Heat-Shock Proteins / Q000737:chemistry* / Q000648:ultrastructure*; D007091:Image Processing, Computer-Assisted / Q000379:methods*; D018625:Microscopy, Atomic Force / Q000379:methods*; D018832:Molecular Chaperones / Q000737:chemistry* / Q000648:ultrastructure*; D011487:Protein Conformation; D016944:Sulfolobus / Q000737:chemistry / Q000648:ultrastructure*
D019843:Archaeal Proteins; D006360:Heat-Shock Proteins; D018832:Molecular Chaperones; C072010:TF55 protein, Sulfolobus shibatae; D018833:Chaperonins