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Volumn 103, Issue 4, 2012, Pages 807-816

Engineered Bi-histidine metal chelation sites map the structure of the mechanical unfolding transition state of an elastomeric protein domain GB1

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; ELASTOMER; HISTIDINE; IGG FC BINDING PROTEIN, STREPTOCOCCUS; IGG FC-BINDING PROTEIN, STREPTOCOCCUS; NICKEL;

EID: 84865357128     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1016/j.bpj.2012.07.019     Document Type: Article
Times cited : (14)

References (43)
  • 1
    • 66849106554 scopus 로고    scopus 로고
    • An expanding arsenal of experimental methods yields an explosion of insights into protein folding mechanisms
    • A.I. Bartlett, and S.E. Radford An expanding arsenal of experimental methods yields an explosion of insights into protein folding mechanisms Nat. Struct. Mol. Biol. 16 2009 582 588
    • (2009) Nat. Struct. Mol. Biol. , vol.16 , pp. 582-588
    • Bartlett, A.I.1    Radford, S.E.2
  • 2
    • 0037154980 scopus 로고    scopus 로고
    • Protein folding and unfolding at atomic resolution
    • DOI 10.1016/S0092-8674(02)00620-7
    • A.R. Fersht, and V. Daggett Protein folding and unfolding at atomic resolution Cell 108 2002 573 582 (Pubitemid 34260881)
    • (2002) Cell , vol.108 , Issue.4 , pp. 573-582
    • Fersht, A.R.1    Daggett, V.2
  • 4
    • 0026511656 scopus 로고
    • The folding of an enzyme. I. Theory of protein engineering analysis of stability and pathway of protein folding
    • A.R. Fersht, A. Matouschek, and L. Serrano The folding of an enzyme. I. Theory of protein engineering analysis of stability and pathway of protein folding J. Mol. Biol. 224 1992 771 782
    • (1992) J. Mol. Biol. , vol.224 , pp. 771-782
    • Fersht, A.R.1    Matouschek, A.2    Serrano, L.3
  • 5
    • 0024358426 scopus 로고
    • Mapping the transition state and pathway of protein folding by protein engineering
    • DOI 10.1038/340122a0
    • A. Matouschek, and J.T. Kellis Jr. A.R. Fersht Mapping the transition state and pathway of protein folding by protein engineering Nature 340 1989 122 126 (Pubitemid 19175363)
    • (1989) Nature , vol.340 , Issue.6229 , pp. 122-126
    • Matouschek, A.1    Kellis Jr., J.T.2    Serrano, L.3    Fersht, A.R.4
  • 6
    • 1442348207 scopus 로고    scopus 로고
    • Discerning the structure and energy of multiple transition states in protein folding using ψ-analysis
    • B.A. Krantz, R.S. Dothager, and T.R. Sosnick Discerning the structure and energy of multiple transition states in protein folding using ψ-analysis J. Mol. Biol. 347 2005 463 475
    • (2005) J. Mol. Biol. , vol.347 , pp. 463-475
    • Krantz, B.A.1    Dothager, R.S.2    Sosnick, T.R.3
  • 7
    • 0035191642 scopus 로고    scopus 로고
    • Engineered metal binding sites map the heterogeneous folding landscape of a coiled coil
    • DOI 10.1038/nsb723
    • B.A. Krantz, and T.R. Sosnick Engineered metal binding sites map the heterogeneous folding landscape of a coiled coil Nat. Struct. Biol. 8 2001 1042 1047 (Pubitemid 33101624)
    • (2001) Nature Structural Biology , vol.8 , Issue.12 , pp. 1042-1047
    • Krantz, B.A.1    Sosnick, T.R.2
  • 8
    • 33646935188 scopus 로고    scopus 로고
    • Characterizing the protein folding transition state using χ analysis
    • DOI 10.1021/cr040431q
    • T.R. Sosnick, and B.A. Krantz M. Baxa Characterizing the protein folding transition state using ψ analysis Chem. Rev. 106 2006 1862 1876 (Pubitemid 43792783)
    • (2006) Chemical Reviews , vol.106 , Issue.5 , pp. 1862-1876
    • Sosnick, T.R.1    Krantz, B.A.2    Dothager, R.S.3    Baxa, M.4
  • 10
    • 0033817704 scopus 로고    scopus 로고
    • Stretching single molecules into novel conformations using the atomic force microscope
    • T.E. Fisher, P.E. Marszalek, and J.M. Fernandez Stretching single molecules into novel conformations using the atomic force microscope Nat. Struct. Biol. 7 2000 719 724
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 719-724
    • Fisher, T.E.1    Marszalek, P.E.2    Fernandez, J.M.3
  • 12
    • 43749107950 scopus 로고    scopus 로고
    • Mechanical biochemistry of proteins one molecule at a time
    • A.F. Oberhauser, and M. Carrión-Vázquez Mechanical biochemistry of proteins one molecule at a time J. Biol. Chem. 283 2008 6617 6621
    • (2008) J. Biol. Chem. , vol.283 , pp. 6617-6621
    • Oberhauser, A.F.1    Carrión-Vázquez, M.2
  • 14
    • 0042744701 scopus 로고    scopus 로고
    • Mechanical unfolding of a titin Ig domain: Structure of transition state revealed by combining atomic force microscopy, protein engineering and molecular dynamics simulations
    • R.B. Best, and S.B. Fowler J. Clarke Mechanical unfolding of a titin Ig domain: structure of transition state revealed by combining atomic force microscopy, protein engineering and molecular dynamics simulations J. Mol. Biol. 330 2003 867 877
    • (2003) J. Mol. Biol. , vol.330 , pp. 867-877
    • Best, R.B.1    Fowlerclarke, J.S.B.2
  • 15
    • 0037126019 scopus 로고    scopus 로고
    • A simple method for probing the mechanical unfolding pathway of proteins in detail
    • R.B. Best, and S.B. Fowler J. Clarke A simple method for probing the mechanical unfolding pathway of proteins in detail Proc. Natl. Acad. Sci. USA 99 2002 12143 12148
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 12143-12148
    • Best, R.B.1    Fowlerclarke, J.S.B.2
  • 16
    • 20544465799 scopus 로고    scopus 로고
    • Mechanical unfolding of TNfn3: The unfolding pathway of a fnIII domain probed by protein engineering, AFM and MD simulation
    • DOI 10.1016/j.jmb.2005.04.070, PII S0022283605005036
    • S.P. Ng, and R.W. Rounsevell J. Clarke Mechanical unfolding of TNfn3: the unfolding pathway of a fnIII domain probed by protein engineering, AFM and MD simulation J. Mol. Biol. 350 2005 776 789 (Pubitemid 40848674)
    • (2005) Journal of Molecular Biology , vol.350 , Issue.4 , pp. 776-789
    • Ng, S.P.1    Rounsevell, R.W.S.2    Steward, A.3    Geierhaas, C.D.4    Williams, P.M.5    Paci, E.6    Clarke, J.7
  • 17
    • 70349233748 scopus 로고    scopus 로고
    • Identification of a mechanical rheostat in the hydrophobic core of protein L
    • D.P. Sadler, and E. Petrik D.J. Brockwell Identification of a mechanical rheostat in the hydrophobic core of protein L J. Mol. Biol. 393 2009 237 248
    • (2009) J. Mol. Biol. , vol.393 , pp. 237-248
    • Sadler, D.P.1    Petrikbrockwell, D.J.E.2
  • 18
    • 73349117815 scopus 로고    scopus 로고
    • Mechanical signaling on the single protein level studied using steered molecular dynamics
    • G.Z. Genchev, and M. Källberg H. Lu Mechanical signaling on the single protein level studied using steered molecular dynamics Cell Biochem. Biophys. 55 2009 141 152
    • (2009) Cell Biochem. Biophys. , vol.55 , pp. 141-152
    • Genchev, G.Z.1    Källberglu, H.M.2
  • 19
    • 70349779536 scopus 로고    scopus 로고
    • Discovery through the computational microscope
    • E.H. Lee, and J. Hsin K. Schulten Discovery through the computational microscope Structure 17 2009 1295 1306
    • (2009) Structure , vol.17 , pp. 1295-1306
    • Lee, E.H.1    Hsinschulten, K.J.2
  • 20
    • 34249930159 scopus 로고    scopus 로고
    • Single-molecule experiments in vitro and in silico
    • DOI 10.1126/science.1137591
    • M. Sotomayor, and K. Schulten Single-molecule experiments in vitro and in silico Science 316 2007 1144 1148 (Pubitemid 46877468)
    • (2007) Science , vol.316 , Issue.5828 , pp. 1144-1148
    • Sotomayor, M.1    Schulten, K.2
  • 21
    • 0025730892 scopus 로고
    • Engineered metal-binding proteins: Purification to protein folding
    • F.H. Arnold, and B.L. Haymore Engineered metal-binding proteins: purification to protein folding Science 252 1991 1796 1797
    • (1991) Science , vol.252 , pp. 1796-1797
    • Arnold, F.H.1    Haymore, B.L.2
  • 23
    • 49649083370 scopus 로고    scopus 로고
    • Single molecule force spectroscopy reveals engineered metal chelation is a general approach to enhance mechanical stability of proteins
    • Y. Cao, T. Yoo, and H.B. Li Single molecule force spectroscopy reveals engineered metal chelation is a general approach to enhance mechanical stability of proteins Proc. Natl. Acad. Sci. USA 105 2008 11152 11157
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 11152-11157
    • Cao, Y.1    Yoo, T.2    Li, H.B.3
  • 24
    • 67650069571 scopus 로고    scopus 로고
    • A force-spectroscopy-based single-molecule metal-binding assay
    • Y. Cao, and K.S. Er H. Li A force-spectroscopy-based single-molecule metal-binding assay ChemPhysChem 10 2009 1450 1454
    • (2009) ChemPhysChem , vol.10 , pp. 1450-1454
    • Cao, Y.1    Erli, H.K.S.2
  • 25
    • 33847273015 scopus 로고    scopus 로고
    • Force denaturation of proteins - An unfolding story
    • D.J. Brockwell Force denaturation of proteins - an unfolding story Curr. Nanosci 3 2007 3 15 (Pubitemid 46322299)
    • (2007) Current Nanoscience , vol.3 , Issue.1 , pp. 3-15
    • Brockwell, D.J.1
  • 27
    • 53849090669 scopus 로고    scopus 로고
    • 'Mechanical engineering' of elastomeric proteins: Toward designing new protein building blocks for biomaterials
    • H.B. Li 'Mechanical engineering' of elastomeric proteins: toward designing new protein building blocks for biomaterials Adv. Funct. Mater. 18 2008 2643 2657
    • (2008) Adv. Funct. Mater. , vol.18 , pp. 2643-2657
    • Li, H.B.1
  • 28
    • 0034804341 scopus 로고    scopus 로고
    • Can non-mechanical proteins withstand force? Stretching barnase by atomic force microscopy and molecular dynamics simulation
    • R.B. Best, and B. Li J. Clarke Can non-mechanical proteins withstand force? Stretching barnase by atomic force microscopy and molecular dynamics simulation Biophys. J. 81 2001 2344 2356 (Pubitemid 32917181)
    • (2001) Biophysical Journal , vol.81 , Issue.4 , pp. 2344-2356
    • Best, R.B.1    Li, B.2    Steward, A.3    Daggett, V.4    Clarke, J.5
  • 29
    • 33846666463 scopus 로고    scopus 로고
    • Polyprotein of GB1 is an ideal artificial elastomeric protein
    • DOI 10.1038/nmat1825, PII NMAT1825
    • Y. Cao, and H.B. Li Polyprotein of GB1 is an ideal artificial elastomeric protein Nat. Mater. 6 2007 109 114 (Pubitemid 46197646)
    • (2007) Nature Materials , vol.6 , Issue.2 , pp. 109-114
    • Cao, Y.1    Li, H.2
  • 30
    • 11544281834 scopus 로고    scopus 로고
    • Elastically coupled two-level systems as a model for biopolymer extensibility
    • M. Rief, J.M. Fernandez, and H.E. Gaub Elastically coupled two-level systems as a model for biopolymer extensibility Phys. Rev. Lett. 81 1998 4764 4767 (Pubitemid 128626983)
    • (1998) Physical Review Letters , vol.81 , Issue.21 , pp. 4764-4767
    • Rief, M.1    Fernandez, J.M.2    Gaub, H.E.3
  • 31
    • 0032516205 scopus 로고    scopus 로고
    • The molecular elasticity of the extracellular matrix protein tenascin
    • DOI 10.1038/30270
    • A.F. Oberhauser, and P.E. Marszalek J.M. Fernandez The molecular elasticity of the extracellular matrix protein tenascin Nature 393 1998 181 185 (Pubitemid 28242260)
    • (1998) Nature , vol.393 , Issue.6681 , pp. 181-185
    • Oberhauser, A.F.1    Marszalek, P.E.2    Erickson, H.P.3    Fernandez, J.M.4
  • 33
    • 0027411181 scopus 로고
    • Thermodynamic β-sheet propensities measured using a zinc-finger host peptide
    • DOI 10.1038/362267a0
    • C.A. Kim, and J.M. Berg Thermodynamic β-sheet propensities measured using a zinc-finger host peptide Nature 362 1993 267 270 (Pubitemid 23093636)
    • (1993) Nature , vol.362 , Issue.6417 , pp. 267-270
    • Kim, C.A.1    Berg, J.M.2
  • 34
    • 0033871567 scopus 로고    scopus 로고
    • Critical role of β-hairpin formation in protein G folding
    • DOI 10.1038/77971
    • E.L. McCallister, E. Alm, and D. Baker Critical role of β-hairpin formation in protein G folding Nat. Struct. Biol. 7 2000 669 673 (Pubitemid 30636679)
    • (2000) Nature Structural Biology , vol.7 , Issue.8 , pp. 669-673
    • McCallister, E.L.1    Alm, E.2    Baker, D.3
  • 35
    • 0034964196 scopus 로고    scopus 로고
    • Computer-based redesign of a protein folding pathway
    • DOI 10.1038/89638
    • S. Nauli, B. Kuhlman, and D. Baker Computer-based redesign of a protein folding pathway Nat. Struct. Biol. 8 2001 602 605 (Pubitemid 32613008)
    • (2001) Nature Structural Biology , vol.8 , Issue.7 , pp. 602-605
    • Nauli, S.1    Kuhlman, B.2    Baker, D.3
  • 36
    • 0028500779 scopus 로고
    • A short linear peptide that folds into a native stable β-hairpin in aqueous solution
    • F.J. Blanco, G. Rivas, and L. Serrano A short linear peptide that folds into a native stable β-hairpin in aqueous solution Nat. Struct. Biol. 1 1994 584 590
    • (1994) Nat. Struct. Biol. , vol.1 , pp. 584-590
    • Blanco, F.J.1    Rivas, G.2    Serrano, L.3
  • 37
    • 79951529367 scopus 로고    scopus 로고
    • Force-induced change in protein unfolding mechanism: Discrete or continuous switch?
    • T.G. Graham, and R.B. Best Force-induced change in protein unfolding mechanism: discrete or continuous switch? J. Phys. Chem. B 115 2011 1546 1561
    • (2011) J. Phys. Chem. B , vol.115 , pp. 1546-1561
    • Graham, T.G.1    Best, R.B.2
  • 38
    • 68249162307 scopus 로고    scopus 로고
    • Mechanical unfolding of proteins L and G with constant force: Similarities and differences
    • A.V. Glyakina, N.K. Balabaev, and O.V. Galzitskaya Mechanical unfolding of proteins L and G with constant force: similarities and differences J. Chem. Phys. 131 2009 045102
    • (2009) J. Chem. Phys. , vol.131 , pp. 045102
    • Glyakina, A.V.1    Balabaev, N.K.2    Galzitskaya, O.V.3
  • 39
    • 65549157601 scopus 로고    scopus 로고
    • Comparison of transition states obtained upon modeling of unfolding of immunoglobulin-binding domains of proteins L and G caused by external action with transition states obtained in the absence of force probed by experiments
    • A.V. Glyakina, N.K. Balabaev, and O.V. Galzitskaya Comparison of transition states obtained upon modeling of unfolding of immunoglobulin-binding domains of proteins L and G caused by external action with transition states obtained in the absence of force probed by experiments Biochemistry (Mosc.) 74 2009 316 328
    • (2009) Biochemistry (Mosc.) , vol.74 , pp. 316-328
    • Glyakina, A.V.1    Balabaev, N.K.2    Galzitskaya, O.V.3
  • 40
    • 1642444204 scopus 로고    scopus 로고
    • Ubiquitin-like protein domains show high resistance to mechanical unfolding similar to that of the 127 domain in titin: Evidence from simulations
    • P.C. Li, and D.E. Makarov Ubiquitin-like protein domains show high resistance to mechanical unfolding similar to that of the 127 domain in titin: evidence from simulations J. Phys. Chem. B 108 2004 745 749
    • (2004) J. Phys. Chem. B , vol.108 , pp. 745-749
    • Li, P.C.1    Makarov, D.E.2
  • 41
    • 0028354429 scopus 로고
    • Two crystal structures of the B1 immunoglobulin-binding domain of streptococcal protein G and comparison with NMR
    • T. Gallagher, and P. Alexander G.L. Gilliland Two crystal structures of the B1 immunoglobulin-binding domain of streptococcal protein G and comparison with NMR Biochemistry 33 1994 4721 4729 (Pubitemid 24145123)
    • (1994) Biochemistry , vol.33 , Issue.15 , pp. 4721-4729
    • Gallagher, T.1    Alexander, P.2    Bryan, P.3    Gilliland, G.L.4


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