Hidden dynamics in the unfolding of individual bacteriorhodopsin proteins

Science

Volumn 355, Issue 6328, 2017, Pages 945-950

  Yu, Hao ^a   Siewny, Matthew G W ^a   Edwards, Devin T ^a   Sanders, Aric W ^b   Perkins, Thomas T ^a  

^a UNIVERSITY OF COLORADO   (United States)

^b NATIONAL INSTITUTE OF STANDARDS AND TECHNOLOGY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; BACTERIORHODOPSIN; MEMBRANE PROTEIN; LIPID BILAYER;

AMINO ACID; EQUILIBRIUM; EXPERIMENTAL STUDY; INSTRUMENTATION; LIPID; MEMBRANE; PROTEIN; SPECTROSCOPY;

ARTICLE; LIPID BILAYER; MOLECULAR DYNAMICS; PRIORITY JOURNAL; PROTEIN REFOLDING; PROTEIN UNFOLDING; SPATIOTEMPORAL ANALYSIS; SPECTROSCOPY; ATOMIC FORCE MICROSCOPY; BETA SHEET; CHEMISTRY; SINGLE MOLECULE IMAGING;

BACTERIORHODOPSINS; LIPID BILAYERS; MICROSCOPY, ATOMIC FORCE; PROTEIN CONFORMATION, BETA-STRAND; PROTEIN UNFOLDING; SINGLE MOLECULE IMAGING;

EID: 85014666991     PISSN: 00368075     EISSN: 10959203     Source Type: Journal    
DOI: 10.1126/science.aah7124     Document Type: Article

References (40)

1. K. A. Dill, J. L. MacCallum, Science 338, 1042-1046 (2012).
2. D. M. Korzhnev, T. L. Religa, W. Banachewicz, A. R. Fersht, L. E. Kay, Science 329, 1312-1316 (2010).
3. X. Zhuang et al., Science 288, 2048-2051 (2000).
4. A. Borgia, P. M. Williams, J. Clarke, Annu. Rev. Biochem. 77, 101-125 (2008).
5. P. E. Marszalek et al., Nature 402, 100-103 (1999).
6. J. Liphardt, B. Onoa, S. B. Smith, I. Tinoco Jr., C. Bustamante, Science 292, 733-737 (2001).
7. C. Cecconi, E. A. Shank, C. Bustamante, S. Marqusee, Science 309, 2057-2060 (2005).
8. J. Stigler, F. Ziegler, A. Gieseke, J. C. M. Gebhardt, M. Rief, Science 334, 512-516 (2011).
9. F. Oesterhelt et al., Science 288, 143-146 (2000).
10. Y. Gao et al., Science 337, 1340-1343 (2012).
11. B. Onoa et al., Science 299, 1892-1895 (2003).
12. G. M. Nam, D. E. Makarov, Protein Sci. 25, 123-134 (2016).
13. P. Cossio, G. Hummer, A. Szabo, Proc. Natl. Acad. Sci. U.S.A. 112, 14248-14253 (2015).
14. K. C. Neuman, A. Nagy, Nat. Methods 5, 491-505 (2008).
15. K. Neupane et al., Science 352, 239-242 (2016).
16. F. Rico, L. Gonzalez, I. Casuso, M. Puig-Vidal, S. Scheuring, Science 342, 741-743 (2013).
17. D. T. Edwards et al., Nano Lett. 15, 7091-7098 (2015).
18. D. J. Müller et al., Biophys. J. 83, 3578-3588 (2002).
19. C. A. Bippes, D. J. Muller, Rep. Prog. Phys. 74, 086601 (2011).
20. K. T. Sapra, H. Besir, D. Oesterhelt, D. J. Muller, J. Mol. Biol. 355, 640-650 (2006).
21. R. Petrosyan et al., Nano Lett. 15, 3624-3633 (2015).
22. M. Zocher et al., ACS Nano 6, 961-971 (2012).
23. C. Kappel, H. Grubmüller, Biophys. J. 100, 1109-1119 (2011).
24. M. Jahn, J. Buchner, T. Hugel, M. Rief, Proc. Natl. Acad. Sci. U.S.A. 113, 1232-1237 (2016).
25. H. S. Chung, K. McHale, J. M. Louis, W. A. Eaton, Science 335, 981-984 (2012).
26. M. Kessler, K. E. Gottschalk, H. Janovjak, D. J. Muller, H. E. Gaub, J. Mol. Biol. 357, 644-654 (2006).
27. J. P. Junker, F. Ziegler, M. Rief, Science 323, 633-637 (2009).
28. C. He et al., Angew. Chem. Int. Ed. Engl. 54, 9921-9925 (2015).
29. M. T. Woodside, S. M. Block, Annu. Rev. Biophys. 43, 19-39 (2014).
30. Y. Zhang, O. K. Dudko, Proc. Natl. Acad. Sci. U.S.A. 110, 16432-16437 (2013).
31. Y. M. Rhee, V. S. Pande, J. Phys. Chem. B 109, 6780-6786 (2005).
32. A. P. Manuel, J. Lambert, M. T. Woodside, Proc. Natl. Acad. Sci. U.S.A. 112, 7183-7188 (2015).
33. J. Preiner et al., Biophys. J. 93, 930-937 (2007).
34. F. Cymer, G. von Heijne, S. H. White, J. Mol. Biol. 427, 999-1022 (2015).
35. G. von Heijne, Nat. Rev. Mol. Cell Biol. 7, 909-918 (2006).
36. M. T. Woodside et al., Science 314, 1001-1004 (2006).
37. G. I. Bell, Science 200, 618-627 (1978).
38. O. K. Dudko, G. Hummer, A. Szabo, Phys. Rev. Lett. 96, 108101 (2006).
39. A. Savinov, C. F. Perez, S. M. Block, Biochim. Biophys. Acta 1839, 1030-1045 (2014).
40. E. M. Puchner, H. E. Gaub, Annu. Rev. Biophys. 41, 497-518 (2012).