DOI: 10.1073/pnas.94.15.7937. Microsecond atomic force sensing of protein conformational dynamics: Implications for the primary light-induced events in bacteriorhodopsin

Microsecond atomic force sensing of protein conformational dynamics: Implications for the primary light-induced events in bacteriorhodopsin

10.1073/pnas.94.15.7937

Crossref journal-article

Proceedings of the National Academy of Sciences

Proceedings of the National Academy of Sciences (341)

Abstract

In this paper a new atomic force sensing technique is presented for dynamically probing conformational changes in proteins. The method is applied to the light-induced changes in the membrane-bound proton pump bacteriorhodopsin (bR). The microsecond time-resolution of the method, as presently implemented, covers many of the intermediates of the bR photocycle which is well characterized by spectroscopical methods. In addition to the native pigment, we have studied bR proteins substituted with chemically modified retinal chromophores. These synthetic chromophores were designed to restrict their ability to isomerize, while maintaining the basic characteristic of a large light-induced charge redistribution in the vertically excited Franck–Condon state. An analysis of the atomic force sensing signals lead us to conclude that protein conformational changes in bR can be initiated as a result of a light-triggered redistribution of electronic charge in the retinal chromophore, even when isomerization cannot take place. Although the coupling mechanism of such changes to the light-induced proton pump is still not established, our data question the current working hypothesis which attributes all primary events in retinal proteins to an initial trans ⇔ cis isomerization.

Bibliography

Rousso, I., Khachatryan, E., Gat, Y., Brodsky, I., Ottolenghi, M., Sheves, M., & Lewis, A. (1997). Microsecond atomic force sensing of protein conformational dynamics: Implications for the primary light-induced events inâbacteriorhodopsin. Proceedings of the National Academy of Sciences, 94(15), 7937â7941.

Authors 7

Itay Rousso (first)
Edward Khachatryan (additional)
Yahaloma Gat (additional)
Igor Brodsky (additional)
Michael Ottolenghi (additional)
Mordechai Sheves (additional)
Aaron Lewis (additional)

References 41 Referenced 59

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A Lewis, I Rousso, E Khachatryan, I Brodsky, K Lieberman, M Sheves Biophys J 70, 2350–2384 (1996). / Biophys J by Lewis A (1996)
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Dates

Type	When
Created	23 years ago (July 26, 2002, 10:35 a.m.)
Deposited	3 years, 4 months ago (April 13, 2022, 3:15 p.m.)
Indexed	2 months, 1 week ago (June 12, 2025, 3:50 a.m.)
Issued	28 years, 1 month ago (July 22, 1997)
Published	28 years, 1 month ago (July 22, 1997)
Published Online	28 years, 1 month ago (July 22, 1997)
Published Print	28 years, 1 month ago (July 22, 1997)

Funders 0

None

BibTeX

@article{Rousso_1997, title={Microsecond atomic force sensing of protein conformational dynamics: Implications for the primary light-induced events in bacteriorhodopsin}, volume={94}, ISSN={1091-6490}, url={http://dx.doi.org/10.1073/pnas.94.15.7937}, DOI={10.1073/pnas.94.15.7937}, number={15}, journal={Proceedings of the National Academy of Sciences}, publisher={Proceedings of the National Academy of Sciences}, author={Rousso, Itay and Khachatryan, Edward and Gat, Yahaloma and Brodsky, Igor and Ottolenghi, Michael and Sheves, Mordechai and Lewis, Aaron}, year={1997}, month=jul, pages={7937–7941} }

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