Directly probing rapid membrane protein dynamics with an atomic force microscope: A study of light-induced conformational alterations in bacteriorhodopsin

Aaron Lewis, Itay Rousso, Edward Khachatryan, Igor Brodsky, Klony Lieberman, Mordechai Sheves

Research output: Contribution to journalArticlepeer-review

17 Scopus citations

Abstract

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.

Original languageEnglish
Pages (from-to)2380-2384
Number of pages5
JournalBiophysical Journal
Volume70
Issue number5
DOIs
StatePublished - 1 Jan 1996
Externally publishedYes

ASJC Scopus subject areas

  • Biophysics

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