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Volumn 93, Issue 3, 2007, Pages 930-937

Free energy of membrane protein unfolding derived from single-molecule force measurements

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIORHODOPSIN; HALORHODOPSIN; MEMBRANE PROTEIN; SODIUM PROTON ANTIPORTER NHAA; SODIUM PROTON EXCHANGE PROTEIN; UNCLASSIFIED DRUG;

EID: 34547679932     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1529/biophysj.106.096982     Document Type: Article
Times cited : (39)

References (49)
  • 1
    • 0031954925 scopus 로고    scopus 로고
    • Genome-wide analysis of integral membrane proteins from eubacterial, archaean, and eukaryotic organisms
    • Wallin, E., and G. von Heijne. 1998. Genome-wide analysis of integral membrane proteins from eubacterial, archaean, and eukaryotic organisms. Protein Sci. 7:1029-1038.
    • (1998) Protein Sci , vol.7 , pp. 1029-1038
    • Wallin, E.1    von Heijne, G.2
  • 2
    • 28444488355 scopus 로고    scopus 로고
    • Solving the membrane protein folding problem
    • Bowie, J. U. 2005. Solving the membrane protein folding problem. Nature. 438:581-589.
    • (2005) Nature , vol.438 , pp. 581-589
    • Bowie, J.U.1
  • 3
    • 27144549973 scopus 로고    scopus 로고
    • Sequential triage of transmembrane segments by Sec61α during biogenesis of a native multispanning membrane protein
    • Sadlish, H., D. Pitonzo, A. E. Johnson, and W. R. Skach. 2005. Sequential triage of transmembrane segments by Sec61α during biogenesis of a native multispanning membrane protein. Nat. Struct. Mol. Biol. 12:870-878.
    • (2005) Nat. Struct. Mol. Biol , vol.12 , pp. 870-878
    • Sadlish, H.1    Pitonzo, D.2    Johnson, A.E.3    Skach, W.R.4
  • 4
    • 0001041988 scopus 로고    scopus 로고
    • Probing the folding and unfolding of wild-type and mutant forms of bacteriorhodopsin in micellar solutions: Evaluation of reversible unfolding conditions
    • Chen, G. Q., and E. Gouaux. 1999. Probing the folding and unfolding of wild-type and mutant forms of bacteriorhodopsin in micellar solutions: evaluation of reversible unfolding conditions. Biochemistry. 38:15380-15387.
    • (1999) Biochemistry , vol.38 , pp. 15380-15387
    • Chen, G.Q.1    Gouaux, E.2
  • 5
    • 0026611771 scopus 로고
    • The role of retinal in the thermal stability of the purple membrane
    • Cladera, J., M. L. Galisteo, M. Sabes, P. L. Mateo, and E. Padros. 1992. The role of retinal in the thermal stability of the purple membrane. Eur. J. Biochem. 207:581-585.
    • (1992) Eur. J. Biochem , vol.207 , pp. 581-585
    • Cladera, J.1    Galisteo, M.L.2    Sabes, M.3    Mateo, P.L.4    Padros, E.5
  • 6
    • 0027300586 scopus 로고
    • Thermal transitions in the purple membrane from Halobacterium halobium
    • Shnyrov, V. L., and P. L. Mateo. 1993. Thermal transitions in the purple membrane from Halobacterium halobium. FEBS Lett. 324:237-240.
    • (1993) FEBS Lett , vol.324 , pp. 237-240
    • Shnyrov, V.L.1    Mateo, P.L.2
  • 7
    • 0029032977 scopus 로고
    • A pathway for the thermal destabilization of bacteriorhodopsin
    • Taneva, S. G., J. M. Caaveiro, A. Muga, and F. M. Goni. 1995. A pathway for the thermal destabilization of bacteriorhodopsin. FEBS Lett. 367:297-300.
    • (1995) FEBS Lett , vol.367 , pp. 297-300
    • Taneva, S.G.1    Caaveiro, J.M.2    Muga, A.3    Goni, F.M.4
  • 8
    • 0032987478 scopus 로고    scopus 로고
    • Membrane protein folding and stability: Physical principles
    • White, S. H., and W. C. Wimley. 1999. Membrane protein folding and stability: physical principles. Annu. Rev. Biophys. Biomol. Struct. 28:319-365.
    • (1999) Annu. Rev. Biophys. Biomol. Struct , vol.28 , pp. 319-365
    • White, S.H.1    Wimley, W.C.2
  • 10
    • 0037066262 scopus 로고    scopus 로고
    • Force spectroscopy of single biomolecules
    • Rief, M., and H. Grubmuller. 2002. Force spectroscopy of single biomolecules. Chem. Phys. Chem. 3:255-261.
    • (2002) Chem. Phys. Chem , vol.3 , pp. 255-261
    • Rief, M.1    Grubmuller, H.2
  • 11
    • 0034665438 scopus 로고    scopus 로고
    • Force spectroscopy of molecular systems. Single-molecule spectroscopy of polymers and biomolecules
    • Janshoff, A., M. Neitzert, Y. Oberdorfer, and H. Fuchs. 2000. Force spectroscopy of molecular systems. Single-molecule spectroscopy of polymers and biomolecules. Angew. Chem. Int. Ed. Engl. 39:3212-3237.
    • (2000) Angew. Chem. Int. Ed. Engl , vol.39 , pp. 3212-3237
    • Janshoff, A.1    Neitzert, M.2    Oberdorfer, Y.3    Fuchs, H.4
  • 14
    • 0036932510 scopus 로고    scopus 로고
    • Stability of bacteriorhodopsin α-helices and loops analyzed by single-molecule force spectroscopy
    • Muller, D. J., M. Kessler, F. Oesterhelt, C. Moller, D. Oesterhelt, and H. Gaub. 2002. Stability of bacteriorhodopsin α-helices and loops analyzed by single-molecule force spectroscopy. Biophys. J. 83:3578-3588.
    • (2002) Biophys. J , vol.83 , pp. 3578-3588
    • Muller, D.J.1    Kessler, M.2    Oesterhelt, F.3    Moller, C.4    Oesterhelt, D.5    Gaub, H.6
  • 15
    • 3242796697 scopus 로고    scopus 로고
    • Controlled unfolding and refolding of a single sodium-proton antiporter using atomic force microscopy
    • Kedrov, A., C. Ziegler, H. Janovjak, W. Kühlbrandt, and D. J. Muller. 2004. Controlled unfolding and refolding of a single sodium-proton antiporter using atomic force microscopy. J. Mol. Biol. 340:1143-1152.
    • (2004) J. Mol. Biol , vol.340 , pp. 1143-1152
    • Kedrov, A.1    Ziegler, C.2    Janovjak, H.3    Kühlbrandt, W.4    Muller, D.J.5
  • 16
    • 13844298943 scopus 로고    scopus 로고
    • Probing origins of molecular interactions stabilizing the membrane proteins halorhodopsin and bacteriorhodopsin
    • Cisneros, D. A., D. Oesterhelt, and D. J. Muller. 2005. Probing origins of molecular interactions stabilizing the membrane proteins halorhodopsin and bacteriorhodopsin. Structure. 13:235-242.
    • (2005) Structure , vol.13 , pp. 235-242
    • Cisneros, D.A.1    Oesterhelt, D.2    Muller, D.J.3
  • 17
    • 14744290539 scopus 로고    scopus 로고
    • Single molecule studies of antibody-antigen interaction strength versus intramolecular antigen stability
    • Kienberger, F., G. Kada, H. Mueller, and P. Hinterdorfer. 2005. Single molecule studies of antibody-antigen interaction strength versus intramolecular antigen stability. J. Mol. Biol. 347:597-606.
    • (2005) J. Mol. Biol , vol.347 , pp. 597-606
    • Kienberger, F.1    Kada, G.2    Mueller, H.3    Hinterdorfer, P.4
  • 20
    • 9244234443 scopus 로고    scopus 로고
    • Exploring the energy landscape of GFP by single-molecule mechanical experiments
    • Dietz, H., and M. Rief. 2004. Exploring the energy landscape of GFP by single-molecule mechanical experiments. Proc. Natl. Acad. Sci. USA. 101:16192-16197.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 16192-16197
    • Dietz, H.1    Rief, M.2
  • 21
    • 1842298212 scopus 로고    scopus 로고
    • From Levinthal to pathways to funnels
    • Dill, K. A., and H. S. Chan. 1997. From Levinthal to pathways to funnels. Nat. Struct. Biol. 4:10-19.
    • (1997) Nat. Struct. Biol , vol.4 , pp. 10-19
    • Dill, K.A.1    Chan, H.S.2
  • 22
    • 0028947257 scopus 로고
    • Funnels, pathways, and the energy landscape of protein folding: A synthesis
    • Bryngelson, J. D., J. N. Onuchic, N. D. Socci, and P. G. Wolynes. 1995. Funnels, pathways, and the energy landscape of protein folding: a synthesis. Proteins. 21:167-195.
    • (1995) Proteins , vol.21 , pp. 167-195
    • Bryngelson, J.D.1    Onuchic, J.N.2    Socci, N.D.3    Wolynes, P.G.4
  • 23
    • 4243754128 scopus 로고    scopus 로고
    • Nonequillibrium equality for free energy differences
    • Jarzynski, C. 1997. Nonequillibrium equality for free energy differences. Phys. Rev. Lett. 78:2690-2693.
    • (1997) Phys. Rev. Lett , vol.78 , pp. 2690-2693
    • Jarzynski, C.1
  • 24
    • 0035957434 scopus 로고    scopus 로고
    • Free energy reconstruction from nonequilibrium single-molecule pulling experiments
    • Hummer, G., and A. Szabo. 2001. Free energy reconstruction from nonequilibrium single-molecule pulling experiments. Proc. Natl. Acad. Sci. USA. 98:3658-3661.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 3658-3661
    • Hummer, G.1    Szabo, A.2
  • 25
    • 0037036070 scopus 로고    scopus 로고
    • Equilibrium information from nonequilibrium measurements in an experimental test of Jarzynski's equality
    • Liphardt, J., S. Dumont, S. B. Smith, I. Tinoco, Jr., and C. Bustamante. 2002. Equilibrium information from nonequilibrium measurements in an experimental test of Jarzynski's equality. Science. 296:1832-1835.
    • (2002) Science , vol.296 , pp. 1832-1835
    • Liphardt, J.1    Dumont, S.2    Smith, S.B.3    Tinoco Jr., I.4    Bustamante, C.5
  • 26
    • 23744478437 scopus 로고    scopus 로고
    • Free energy surfaces from single-molecule force spectroscopy
    • Hummer, G., and A. Szabo. 2005. Free energy surfaces from single-molecule force spectroscopy. Acc. Chem. Res. 38:504-513.
    • (2005) Acc. Chem. Res , vol.38 , pp. 504-513
    • Hummer, G.1    Szabo, A.2
  • 27
  • 28
    • 28844490188 scopus 로고    scopus 로고
    • Observing folding pathways and kinetics of a single sodium-proton antiporter from Escherichia coli
    • Kedrov, A., H. Janovjak, C. Ziegler, W. Kuhlbrandt, and D. J. Muller. 2006. Observing folding pathways and kinetics of a single sodium-proton antiporter from Escherichia coli. J. Mol. Biol. 355:2-8.
    • (2006) J. Mol. Biol , vol.355 , pp. 2-8
    • Kedrov, A.1    Janovjak, H.2    Ziegler, C.3    Kuhlbrandt, W.4    Muller, D.J.5
  • 30
    • 0034717007 scopus 로고    scopus 로고
    • Structure of the light-driven chloride pump halorhodopsin at 1.8 Å resolution
    • Kolbe, M., H. Besir, L. O. Essen, and D. Oesterhelt. 2000. Structure of the light-driven chloride pump halorhodopsin at 1.8 Å resolution. Science. 288:1390-1396.
    • (2000) Science , vol.288 , pp. 1390-1396
    • Kolbe, M.1    Besir, H.2    Essen, L.O.3    Oesterhelt, D.4
  • 32
    • 33846264595 scopus 로고    scopus 로고
    • Transmembrane helices have rough energy surfaces
    • Janovjak, H., H. Knaus, and D. J. Muller. 2007. Transmembrane helices have rough energy surfaces. J. Am. Chem. Soc. 129:246-247.
    • (2007) J. Am. Chem. Soc , vol.129 , pp. 246-247
    • Janovjak, H.1    Knaus, H.2    Muller, D.J.3
  • 33
    • 18444364820 scopus 로고    scopus 로고
    • Automated alignment and pattern recognition of single-molecule force spectroscopy data
    • Kuhn, M., H. Janovjak, M. Hubain, and D. J. Muller. 2005. Automated alignment and pattern recognition of single-molecule force spectroscopy data. J. Microsc. 218:125-132.
    • (2005) J. Microsc , vol.218 , pp. 125-132
    • Kuhn, M.1    Janovjak, H.2    Hubain, M.3    Muller, D.J.4
  • 35
    • 85030512941 scopus 로고    scopus 로고
    • Press, W. H., S. A. Teukolsky, W. T. Vetterling, and B. P. Flannery. 1988. Numerical Recipes in C. Cambridge University Press, Cambridge, UK.
    • Press, W. H., S. A. Teukolsky, W. T. Vetterling, and B. P. Flannery. 1988. Numerical Recipes in C. Cambridge University Press, Cambridge, UK.
  • 39
    • 21444445531 scopus 로고    scopus 로고
    • The folding pathway of a fast-folding immunoglobulin domain revealed by single-molecule mechanical experiments
    • 6:46-51
    • Schwaiger, I., M. Schleicher, A. A. Noegel, and M. Rief. 2005. The folding pathway of a fast-folding immunoglobulin domain revealed by single-molecule mechanical experiments. EMBO Rep. 6:46-51.
    • (2005) EMBO Rep
    • Schwaiger, I.1    Schleicher, M.2    Noegel, A.A.3    Rief, M.4
  • 40
    • 0031011695 scopus 로고    scopus 로고
    • Reversible unfolding of individual titin immunoglobulin domains by AFM
    • Rief, M., M. Gautel, F. Oesterhelt, J. M. Fernandez, and H. E. Gaub. 1997. Reversible unfolding of individual titin immunoglobulin domains by AFM. Science. 276:1109-1112.
    • (1997) Science , vol.276 , pp. 1109-1112
    • Rief, M.1    Gautel, M.2    Oesterhelt, F.3    Fernandez, J.M.4    Gaub, H.E.5
  • 42
    • 0141753133 scopus 로고    scopus 로고
    • Unfolding pathways of native bacteriorhodopsin depend on temperature
    • Janovjak, H., M. Kessler, D. Oesterhelt, H. Gaub, and D. J. Muller. 2003. Unfolding pathways of native bacteriorhodopsin depend on temperature. EMBO J. 22:5220-5229.
    • (2003) EMBO J , vol.22 , pp. 5220-5229
    • Janovjak, H.1    Kessler, M.2    Oesterhelt, D.3    Gaub, H.4    Muller, D.J.5
  • 43
    • 17844365575 scopus 로고    scopus 로고
    • Complex stability of single proteins explored by forced unfolding experiments
    • Janovjak, H., K. T. Sapra, and D. J. Muller. 2005. Complex stability of single proteins explored by forced unfolding experiments. Biophys. J. 88:L37-L39.
    • (2005) Biophys. J , vol.88
    • Janovjak, H.1    Sapra, K.T.2    Muller, D.J.3
  • 45
    • 33748467970 scopus 로고    scopus 로고
    • Differentiating ligand and inhibitor interactions of a single antiporter
    • Kedrov, A., C. Ziegler, and D. J. Muller. 2006. Differentiating ligand and inhibitor interactions of a single antiporter. J. Mol. Biol. 362:925-932.
    • (2006) J. Mol. Biol , vol.362 , pp. 925-932
    • Kedrov, A.1    Ziegler, C.2    Muller, D.J.3
  • 46
    • 34347259478 scopus 로고    scopus 로고
    • Deciphering molecular interactions of native membrane proteins by singlemolecule force spectroscopy
    • Kedrov, A., H. Janovjak, K. T. Sapra, and D. J. Muller. 2007. Deciphering molecular interactions of native membrane proteins by singlemolecule force spectroscopy. Annu. Rev. Biophys. Biomol. Struct. 36:233-260.
    • (2007) Annu. Rev. Biophys. Biomol. Struct , vol.36 , pp. 233-260
    • Kedrov, A.1    Janovjak, H.2    Sapra, K.T.3    Muller, D.J.4
  • 48
    • 27744527489 scopus 로고    scopus 로고
    • Unfolding and extraction of a transmembrane α-helical peptide: Dynamic force spectroscopy and molecular dynamics simulations
    • Contera, S. A., V. Lemaitre, M. R. de Planque, A. Watts, and J. F. Ryan. 2005. Unfolding and extraction of a transmembrane α-helical peptide: dynamic force spectroscopy and molecular dynamics simulations. Biophys. J. 89:3129-3140.
    • (2005) Biophys. J , vol.89 , pp. 3129-3140
    • Contera, S.A.1    Lemaitre, V.2    de Planque, M.R.3    Watts, A.4    Ryan, J.F.5
  • 49
    • 9744250110 scopus 로고    scopus 로고
    • Strength of integration of transmembrane α-helical peptides in lipid bilayers as determined by atomic force spectroscopy
    • Ganchev, D. N., D. T. Rijkers, M. M. Snel, J. A. Killian, and B. de Kruijff. 2004. Strength of integration of transmembrane α-helical peptides in lipid bilayers as determined by atomic force spectroscopy. Biochemistry. 43:14987-14993.
    • (2004) Biochemistry , vol.43 , pp. 14987-14993
    • Ganchev, D.N.1    Rijkers, D.T.2    Snel, M.M.3    Killian, J.A.4    de Kruijff, B.5


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