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Volumn 93, Issue 7, 2007, Pages 2436-2446

Force-clamp spectroscopy of single-protein monomers reveals the individual unfolding and folding pathways of i27 and ubiquitin

Author keywords

[No Author keywords available]

Indexed keywords

MONOMER; PROTEIN DERIVATIVE; PROTEIN I 27; UBIQUITIN; UNCLASSIFIED DRUG;

EID: 34848909232     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1529/biophysj.107.104422     Document Type: Article
Times cited : (118)

References (48)
  • 3
    • 33748046806 scopus 로고    scopus 로고
    • Anisotropic deformation response of single protein molecules
    • Dietz, H., F. Berkemeier, M. Bertz, and M. Rief. 2006. Anisotropic deformation response of single protein molecules. Proc. Natl. Acad. Sci. USA. 103:12724-12728.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 12724-12728
    • Dietz, H.1    Berkemeier, F.2    Bertz, M.3    Rief, M.4
  • 4
    • 28444487209 scopus 로고    scopus 로고
    • Fingerprinting single molecules in vivo
    • Fernandez, J. M. 2005. Fingerprinting single molecules in vivo. Biophys. J. 89:3676-3677.
    • (2005) Biophys. J , vol.89 , pp. 3676-3677
    • Fernandez, J.M.1
  • 5
    • 20544435808 scopus 로고    scopus 로고
    • Biophysical investigations of engineered polyproteins: Implications for force data
    • Rounsevell, R. W. S., A. Steward, and J. Clarke. 2005. Biophysical investigations of engineered polyproteins: implications for force data. Biophys. J. 88:2022-2029.
    • (2005) Biophys. J , vol.88 , pp. 2022-2029
    • Rounsevell, R.W.S.1    Steward, A.2    Clarke, J.3
  • 6
    • 0036304229 scopus 로고    scopus 로고
    • Titin; a multidomain protein that behaves as the sum of its parts
    • Scott, K. A., A. Steward, S. B. Fowler, and J. Clarke. 2002. Titin; a multidomain protein that behaves as the sum of its parts. J. Mol. Biol. 315:819-829.
    • (2002) J. Mol. Biol , vol.315 , pp. 819-829
    • Scott, K.A.1    Steward, A.2    Fowler, S.B.3    Clarke, J.4
  • 7
    • 33646000631 scopus 로고    scopus 로고
    • Complex folding kinetics of a multidomain protein
    • Batey, S., K. A. Scott, and J. Clarke. 2006. Complex folding kinetics of a multidomain protein. Biophys. J. 90:2120-2130.
    • (2006) Biophys. J , vol.90 , pp. 2120-2130
    • Batey, S.1    Scott, K.A.2    Clarke, J.3
  • 10
    • 28644437048 scopus 로고    scopus 로고
    • The importance of sequence diversity in the aggregation and evolution of proteins
    • Wright, C. F., S. A. Teichmann, J. Clarke, and C. M. Dobson. 2005. The importance of sequence diversity in the aggregation and evolution of proteins. Nature. 438:878-881.
    • (2005) Nature , vol.438 , pp. 878-881
    • Wright, C.F.1    Teichmann, S.A.2    Clarke, J.3    Dobson, C.M.4
  • 12
    • 7044274259 scopus 로고    scopus 로고
    • Comment on Force-clamp spectroscopy monitors the folding trajectory of a single protein
    • Sosnick, T. R. 2004. Comment on "Force-clamp spectroscopy monitors the folding trajectory of a single protein." Science. 306:411.
    • (2004) Science , vol.306 , pp. 411
    • Sosnick, T.R.1
  • 13
    • 0037337270 scopus 로고    scopus 로고
    • The unfolding story of three-dimensional domain swapping
    • Rousseau, F., J. W. H. Schymkowitz, and L. S. Itzhaki. 2003. The unfolding story of three-dimensional domain swapping. Structure. 11:243-251.
    • (2003) Structure , vol.11 , pp. 243-251
    • Rousseau, F.1    Schymkowitz, J.W.H.2    Itzhaki, L.S.3
  • 15
    • 17844377025 scopus 로고    scopus 로고
    • Comment on "Force-clamp spectroscopy monitors the folding trajectory of a single protein
    • Best, R. B., and G. Hummer. 2005. Comment on "Force-clamp spectroscopy monitors the folding trajectory of a single protein". Science. 308:498.
    • (2005) Science , vol.308 , pp. 498
    • Best, R.B.1    Hummer, G.2
  • 16
    • 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
  • 17
    • 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
  • 18
    • 33845980623 scopus 로고    scopus 로고
    • Mechanical unfolding pathways of the enhanced yellow fluorescent protein (EYFP) revealed by single-molecule force spectroscopy
    • Perez-Jimenez, R., S. Garcia-Manyes, S. Rama Koti Ainavarapu, and J. M. Fernandez. 2006. Mechanical unfolding pathways of the enhanced yellow fluorescent protein (EYFP) revealed by single-molecule force spectroscopy. J. Biol. Chem. 281:40010-40014.
    • (2006) J. Biol. Chem , vol.281 , pp. 40010-40014
    • Perez-Jimenez, R.1    Garcia-Manyes, S.2    Rama Koti Ainavarapu, S.3    Fernandez, J.M.4
  • 19
    • 33748552058 scopus 로고    scopus 로고
    • Engineering proteins with novel mechanical properties by recombination of protein fragments
    • Sharma, D., Y. Cao, and H. B. Li. 2006. Engineering proteins with novel mechanical properties by recombination of protein fragments. Angew. Chem. Int. Ed. Engl. 45:5633-5638.
    • (2006) Angew. Chem. Int. Ed. Engl , vol.45 , pp. 5633-5638
    • Sharma, D.1    Cao, Y.2    Li, H.B.3
  • 20
    • 0031011695 scopus 로고    scopus 로고
    • Reversible unfolding of individual titin immunoglobulin domains by AFM
    • Rief, M., J. Fernandez, and H. 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    Fernandez, J.2    Gaub, H.3
  • 22
    • 0032516205 scopus 로고    scopus 로고
    • The molecular elasticity of the extracellular matrix protein tenascin
    • Oberhauser, A., P. Marszalek, H. Erickson, and J. Fernandez. 1998. The molecular elasticity of the extracellular matrix protein tenascin. Nature. 393:181-185.
    • (1998) Nature , vol.393 , pp. 181-185
    • Oberhauser, A.1    Marszalek, P.2    Erickson, H.3    Fernandez, J.4
  • 23
    • 0033582763 scopus 로고    scopus 로고
    • Single molecule force spectroscopy of spectrin repeats: Low unfolding forces in helix bundles
    • Rief, M., J. Pascual, M. Saraste, and H. E. Gaub. 1999. Single molecule force spectroscopy of spectrin repeats: Low unfolding forces in helix bundles. J. Mol. Biol. 286:553-561.
    • (1999) J. Mol. Biol , vol.286 , pp. 553-561
    • Rief, M.1    Pascual, J.2    Saraste, M.3    Gaub, H.E.4
  • 24
    • 28444470913 scopus 로고    scopus 로고
    • Single adhesive nanofibers from a live diatom have the signature fingerprint of modular proteins
    • Dugdale, T. M., R. Dagastine, A. Chiovitti, P. Mulvaney, and R. Wetherbee. 2005. Single adhesive nanofibers from a live diatom have the signature fingerprint of modular proteins. Biophys. J. 89:4252-4260.
    • (2005) Biophys. J , vol.89 , pp. 4252-4260
    • Dugdale, T.M.1    Dagastine, R.2    Chiovitti, A.3    Mulvaney, P.4    Wetherbee, R.5
  • 26
    • 25444512161 scopus 로고    scopus 로고
    • Direct observation of the three-state folding of a single protein molecule
    • Cecconi, C., E. A. Shank, C. Bustamante, and S. Marqusee. 2005. Direct observation of the three-state folding of a single protein molecule. Science. 309:2057-2060.
    • (2005) Science , vol.309 , pp. 2057-2060
    • Cecconi, C.1    Shank, E.A.2    Bustamante, C.3    Marqusee, S.4
  • 28
    • 2442448427 scopus 로고    scopus 로고
    • The unfolding kinetics of ubiquitin captured with single-molecule force-clamp techniques
    • Schlierf, M., H. Li, and J. Fernandez. 2004. The unfolding kinetics of ubiquitin captured with single-molecule force-clamp techniques. Proc. Natl. Acad. Sci. USA. 101:7299-7304.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 7299-7304
    • Schlierf, M.1    Li, H.2    Fernandez, J.3
  • 29
    • 0018101150 scopus 로고
    • Models for specific adhesion of cells to cells
    • Bell, G. I. 1978. Models for specific adhesion of cells to cells. Science. 200:618-627.
    • (1978) Science , vol.200 , pp. 618-627
    • Bell, G.I.1
  • 30
    • 34147138772 scopus 로고    scopus 로고
    • Dwell-time distribution analysis of polyprotein unfolding using force-clamp spectroscopy
    • Brujic, J., R. I. Hermans, S. Garcia-Manyes, K. A. Walther, and J. M. Fernandez. 2007. Dwell-time distribution analysis of polyprotein unfolding using force-clamp spectroscopy. Biophys. J. 92:2896-2903.
    • (2007) Biophys. J , vol.92 , pp. 2896-2903
    • Brujic, J.1    Hermans, R.I.2    Garcia-Manyes, S.3    Walther, K.A.4    Fernandez, J.M.5
  • 31
    • 33645765218 scopus 로고    scopus 로고
    • Single-molecule force spectroscopy reveals signatures of glassy dynamics in the energy landscape of ubiquitin
    • Brujic, J., R. I. Hermans, K. A. Walther, and J. M. Fernandez. 2006. Single-molecule force spectroscopy reveals signatures of glassy dynamics in the energy landscape of ubiquitin. Nature Physics. 2:282-286.
    • (2006) Nature Physics , vol.2 , pp. 282-286
    • Brujic, J.1    Hermans, R.I.2    Walther, K.A.3    Fernandez, J.M.4
  • 32
    • 22244476443 scopus 로고    scopus 로고
    • Models of traps and glass phenomenology
    • Monthus, C., and J. P. Bouchaud. 1996. Models of traps and glass phenomenology. J Phys a-Math Gen 29:3847-3869.
    • (1996) J Phys a-Math Gen , vol.29 , pp. 3847-3869
    • Monthus, C.1    Bouchaud, J.P.2
  • 33
    • 1542513548 scopus 로고    scopus 로고
    • Force-clamp spectroscopy monitors the folding trajectory of a single protein
    • Fernandez, J., and H. Li. 2004. Force-clamp spectroscopy monitors the folding trajectory of a single protein. Science. 303:1674-1678.
    • (2004) Science , vol.303 , pp. 1674-1678
    • Fernandez, J.1    Li, H.2
  • 34
    • 7044274259 scopus 로고    scopus 로고
    • Response to comment on Force-clamp spectroscopy monitors the folding trajectory of a single protein
    • Fernandez, J., H. Li, and B. J. 2004. Response to comment on "Force-clamp spectroscopy monitors the folding trajectory of a single protein." Science. 306:411c.
    • (2004) Science , vol.306
    • Fernandez, J.1    Li, H.2    J., B.3
  • 35
    • 17844377025 scopus 로고    scopus 로고
    • Response to comment on Force-clamp spectroscopy monitors the folding trajectory of a single protein
    • Brujic, J., and J. W. Fernandez. 2005. Response to comment on "Force-clamp spectroscopy monitors the folding trajectory of a single protein." Science. 308:498.
    • (2005) Science , vol.308 , pp. 498
    • Brujic, J.1    Fernandez, J.W.2
  • 36
    • 0000050196 scopus 로고
    • From minimal models to real proteins: Time scales for protein folding kinetics
    • Thirumalai, D. 1995. From minimal models to real proteins: time scales for protein folding kinetics. J. Phys. I France. 5:1457-1467.
    • (1995) J. Phys. I France , vol.5 , pp. 1457-1467
    • Thirumalai, D.1
  • 37
    • 30444455738 scopus 로고    scopus 로고
    • Multiple stepwise refolding of immunoglobulin domain I27 upon force quench depends on initial conditions
    • Li, M. S., C. K. Hu, D. K. Klimov, and D. Thirumalai. 2006. Multiple stepwise refolding of immunoglobulin domain I27 upon force quench depends on initial conditions. Proc. Natl. Acad. Sci. USA. 103:93-98.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 93-98
    • Li, M.S.1    Hu, C.K.2    Klimov, D.K.3    Thirumalai, D.4
  • 38
    • 34547854222 scopus 로고    scopus 로고
    • Protein folding in a force clamp
    • Cieplak, M., and P. Szymczak. 2006. Protein folding in a force clamp. J. Chem. Phys. 124:194901.
    • (2006) J. Chem. Phys , vol.124 , pp. 194901
    • Cieplak, M.1    Szymczak, P.2
  • 39
    • 33846460423 scopus 로고    scopus 로고
    • Refolding upon force quench and pathways of mechanical and thermal unfolding of ubiquitin
    • Li, M. S., M. Kouza, and C.-K. Hu. 2006. Refolding upon force quench and pathways of mechanical and thermal unfolding of ubiquitin. Biophys. J. 92:547-561.
    • (2006) Biophys. J , vol.92 , pp. 547-561
    • Li, M.S.1    Kouza, M.2    Hu, C.-K.3
  • 40
    • 33847217662 scopus 로고    scopus 로고
    • Fluctuations of primary ubiquitin folding intermediates in a force clamp
    • Grater, F., and H. Grubmuller. 2007. Fluctuations of primary ubiquitin folding intermediates in a force clamp. J. Struct. Biol. 157:557-569.
    • (2007) J. Struct. Biol , vol.157 , pp. 557-569
    • Grater, F.1    Grubmuller, H.2
  • 41
    • 0034685619 scopus 로고    scopus 로고
    • A breakdown of symmetry in the folding transition state of protein L
    • Kim, D. E., C. Fisher, and D. Baker. 2000. A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298:971-984.
    • (2000) J. Mol. Biol , vol.298 , pp. 971-984
    • Kim, D.E.1    Fisher, C.2    Baker, D.3
  • 45
    • 33646547262 scopus 로고    scopus 로고
    • Force-dependent chemical kinetics of disulfide bond reduction observed with single-molecule techniques
    • Wiita, A. P., S. R. K. Ainavarapu, H. H. Huang, and J. M. Fernandez. 2006. Force-dependent chemical kinetics of disulfide bond reduction observed with single-molecule techniques. Proc. Natl. Acad. Sci. USA. 103:7222-7227.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 7222-7227
    • Wiita, A.P.1    Ainavarapu, S.R.K.2    Huang, H.H.3    Fernandez, J.M.4
  • 46
    • 33744802398 scopus 로고    scopus 로고
    • Effects of surface tethering on protein folding mechanisms
    • Friedel, M., A. Baumketner, and J. E. Shea. 2006. Effects of surface tethering on protein folding mechanisms. Proc. Natl. Acad. Sci. USA. 103:8396-8401.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 8396-8401
    • Friedel, M.1    Baumketner, A.2    Shea, J.E.3
  • 48
    • 33646166953 scopus 로고    scopus 로고
    • Sub-angstrom conformational changes of a single molecule captured by AFM variance analysis
    • Walther, K. A., J. Brujic, H. B. Li, and J. M. Fernandez. 2006. Sub-angstrom conformational changes of a single molecule captured by AFM variance analysis. Biophys. J. 90:3806-3812.
    • (2006) Biophys. J , vol.90 , pp. 3806-3812
    • Walther, K.A.1    Brujic, J.2    Li, H.B.3    Fernandez, J.M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.