Directly probing rapid membrane protein dynamics with an atomic force microscope: a study of light-induced conformational alterations in bacteriorhodopsin.
This paper demonstrates that an atomic force microscope can be used to directly monitor rapid membrane protein dynamics. For this demonstration the membrane-bound proton pump, bacteriorhodopsin, has been investigated. It has been unequivocally shown that the light-induced dynamic alterations that have been observed do not arise from external artifacts such as heating of the sample by the incident light, but that these changes can be directly linked to the light-induced protein conformational alterations in this membrane. In essence, it has been shown that the light energy absorbed by bacteriorhodopsin is converted not only to chemical energy but also to mechanical energy. In summary a new ultrasensitive tool is described for monitoring the molecular dynamics of materials with wide applicability to fundamental and applied science.
Lewis
A
A
Division of Applied Physics, The Hebrew University of Jerusalem, Jerusalem, Israel. lewisu@vms.huji.ac.il
Rousso
I
I
Khachatryan
E
E
Brodsky
I
I
Lieberman
K
K
Sheves
M
M
D001436:Bacteriorhodopsins / Q000737:chemistry* / Q000528:radiation effects / Q000648:ultrastructure; D003624:Darkness; D007700:Kinetics; D008027:Light; D008565:Membrane Proteins / Q000737:chemistry*; D018625:Microscopy, Atomic Force / Q000295:instrumentation / Q000379:methods; D009991:Oscillometry; D011487:Protein Conformation; D015203:Reproducibility of Results; D013997:Time Factors
D008565:Membrane Proteins; D001436:Bacteriorhodopsins