메뉴 건너뛰기




Volumn 10, Issue 9, 2003, Pages 731-737

Pulling geometry defines the mechanical resistance of a β-sheet protein

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL ENZYME; BETA SHEET PROTEIN; E2LIP3 PROTEIN; PROTEIN; UNCLASSIFIED DRUG;

EID: 0042508741     PISSN: 10728368     EISSN: None     Source Type: Journal    
DOI: 10.1038/nsb968     Document Type: Article
Times cited : (334)

References (43)
  • 1
    • 0033616713 scopus 로고    scopus 로고
    • Mechanical and chemical unfolding of a single protein: A comparison
    • Carrion-Vazquez, M. et al. Mechanical and chemical unfolding of a single protein: a comparison. Proc. Natl. Acad. Sci. USA 96, 3694-3699 (1999)
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 3694-3699
    • Carrion-Vazquez, M.1
  • 3
    • 0034533671 scopus 로고    scopus 로고
    • Mechanical design of proteins - Studied by single-molecule force spectroscopy and protein engineering
    • Carrion-Vazquez, M. et al. Mechanical design of proteins - studied by single-molecule force spectroscopy and protein engineering. Prog. Biophys. Mol. Biol. 74, 63-91 (2000).
    • (2000) Prog. Biophys. Mol. Biol. , vol.74 , pp. 63-91
    • Carrion-Vazquez, M.1
  • 4
    • 0033151955 scopus 로고    scopus 로고
    • Steered molecular dynamics simulations of force-induced protein domain unfolding
    • Lu, H. & Schulten, K. Steered molecular dynamics simulations of force-induced protein domain unfolding. Proteins 35, 453-463 (1999).
    • (1999) Proteins , vol.35 , pp. 453-463
    • Lu, H.1    Schulten, K.2
  • 5
    • 0034691149 scopus 로고    scopus 로고
    • Native topology determines force-induced unfolding pathways in globular proteins
    • Klimov, D.K. & Thirumalai, D. Native topology determines force-induced unfolding pathways in globular proteins. Proc. Natl. Acad. Sci. USA 97, 7254-7259 (2000).
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 7254-7259
    • Klimov, D.K.1    Thirumalai, D.2
  • 7
    • 0036280490 scopus 로고    scopus 로고
    • The effect of core destabilization on the mechanical resistance of 127
    • Brockwell, D.J. et al. The effect of core destabilization on the mechanical resistance of 127. Biophys. J. 83, 458-472 (2002).
    • (2002) Biophys. J. , vol.83 , pp. 458-472
    • Brockwell, D.J.1
  • 8
    • 0033531973 scopus 로고    scopus 로고
    • Forced unfolding of fibronectin type 3 modules: An analysis by biased molecular dynamics simulations
    • Paci, E. & Karplus, M. Forced unfolding of fibronectin type 3 modules: an analysis by biased molecular dynamics simulations. J. Mol. Biol. 288, 441-459 (1999).
    • (1999) J. Mol. Biol. , vol.288 , pp. 441-459
    • Paci, E.1    Karplus, M.2
  • 9
    • 0034081255 scopus 로고    scopus 로고
    • Mechanical unfolding of a β-hairpin using molecular dynamics
    • Bryant, Z., Pande, V.S. & Rokhsar, D.S. Mechanical unfolding of a β-hairpin using molecular dynamics. Biophys. J. 78, 584-589 (2000).
    • (2000) Biophys. J. , vol.78 , pp. 584-589
    • Bryant, Z.1    Pande, V.S.2    Rokhsar, D.S.3
  • 10
    • 0034713840 scopus 로고    scopus 로고
    • Restricted motion of the lipoyl-lysine swinging arm in the pyruvate dehydrogenase complex of Escherichia coli
    • Jones, D.D., Stott, K.M., Howard, M.J. & Perham, R.N. Restricted motion of the lipoyl-lysine swinging arm in the pyruvate dehydrogenase complex of Escherichia coli. Biochemistry 39, 8448-8459 (2000).
    • (2000) Biochemistry , vol.39 , pp. 8448-8459
    • Jones, D.D.1    Stott, K.M.2    Howard, M.J.3    Perham, R.N.4
  • 11
    • 0033790516 scopus 로고    scopus 로고
    • Swinging arms and swinging domains in multifunctional enzymes: Catalytic machines for multistep reactions
    • Perham, R. N. Swinging arms and swinging domains in multifunctional enzymes: catalytic machines for multistep reactions. Annu. Rev. Biochem. 69, 961-1004 (2000).
    • (2000) Annu. Rev. Biochem. , vol.69 , pp. 961-1004
    • Perham, R.N.1
  • 12
    • 0036891724 scopus 로고    scopus 로고
    • Mechanically unfolding proteins: The effect of unfolding history and the supramolecular scaffold
    • Zinober, R.C. et al. Mechanically unfolding proteins: the effect of unfolding history and the supramolecular scaffold. Protein Sci. 11, 2759-2765 (2002).
    • (2002) Protein Sci. , vol.11 , pp. 2759-2765
    • Zinober, R.C.1
  • 15
    • 0034804341 scopus 로고    scopus 로고
    • Can non-mechanical proteins withstand force? Stretching barnase by atomic force microscopy and molecular dynamics simulation
    • Best, R.B., Li, B., Steward, A., Daggett, V. & Clarke, J. Can non-mechanical proteins withstand force? Stretching barnase by atomic force microscopy and molecular dynamics simulation. Biophys. J. 81, 2344-2356 (2001).
    • (2001) Biophys. J. , vol.81 , pp. 2344-2356
    • Best, R.B.1    Li, B.2    Steward, A.3    Daggett, V.4    Clarke, J.5
  • 16
    • 0031001349 scopus 로고    scopus 로고
    • Dynamic strength of molecular adhesion bonds
    • Evans, E. & Ritchie, K. Dynamic strength of molecular adhesion bonds. Biophys. J. 72, 1541-1555 (1997).
    • (1997) Biophys. J. , vol.72 , pp. 1541-1555
    • Evans, E.1    Ritchie, K.2
  • 18
    • 0033064934 scopus 로고    scopus 로고
    • Unraveling proteins: A molecular mechanics study
    • Rohs, R., Etchebest, C. & Lavery, R. Unraveling proteins: a molecular mechanics study. Biophys. J. 76, 2760-2768 (1999).
    • (1999) Biophys. J. , vol.76 , pp. 2760-2768
    • Rohs, R.1    Etchebest, C.2    Lavery, R.3
  • 19
    • 0033529204 scopus 로고    scopus 로고
    • Atomic levers control pyranose ring conformations
    • Marszalek, P.E. et al. Atomic levers control pyranose ring conformations. Proc. Natl. Acad. Sci. USA 96, 7894-7898 (1999).
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 7894-7898
    • Marszalek, P.E.1
  • 20
    • 0037007051 scopus 로고    scopus 로고
    • Chair-boat transitions in single polysaccharide molecules observed with force-ramp AFM
    • Marszalek, P.E., Li, H.B., Oberhauser, A.F. & Fernandez, J.M. Chair-boat transitions in single polysaccharide molecules observed with force-ramp AFM. Proc. Nat. Acad. Sci. USA 99, 4278-4283 (2002).
    • (2002) Proc. Nat. Acad. Sci. USA , vol.99 , pp. 4278-4283
    • Marszalek, P.E.1    Li, H.B.2    Oberhauser, A.F.3    Fernandez, J.M.4
  • 21
    • 0033523904 scopus 로고    scopus 로고
    • Mechanical unfolding intermediates in titin modules
    • Marszalek, P.E. et al. Mechanical unfolding intermediates in titin modules. Nature 402, 100-103 (1999).
    • (1999) Nature , vol.402 , pp. 100-103
    • Marszalek, P.E.1
  • 22
    • 0036389817 scopus 로고    scopus 로고
    • Mechanical unfolding of a titin Ig domain: Structure of unfolding intermediate revealed by combining AFM, molecular dynamics simulations, NMR and protein engineering
    • Fowler, S.B. et al. Mechanical unfolding of a titin Ig domain: structure of unfolding intermediate revealed by combining AFM, molecular dynamics simulations, NMR and protein engineering. J. Mol. Biol. 322, 841-849 (2002).
    • (2002) J. Mol. Biol. , vol.322 , pp. 841-849
    • Fowler, S.B.1
  • 23
    • 0031848099 scopus 로고    scopus 로고
    • Unfolding of titin immunoglobulin domains by steered molecular dynamics simulation
    • Lu, H., Isralewitz, B., Krammer, A., Vogel, V. & Schulten, K. Unfolding of titin immunoglobulin domains by steered molecular dynamics simulation. Biophys. J. 75, 662-671 (1998).
    • (1998) Biophys. J. , vol.75 , pp. 662-671
    • Lu, H.1    Isralewitz, B.2    Krammer, A.3    Vogel, V.4    Schulten, K.5
  • 24
    • 0034612284 scopus 로고    scopus 로고
    • Unfolding proteins by external forces and temperature: The importance of topology and energetics
    • Paci, E. & Karplus, M. Unfolding proteins by external forces and temperature: the importance of topology and energetics. Proc. Natl. Acad. Sci. USA 97, 6521-6526 (2000).
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 6521-6526
    • Paci, E.1    Karplus, M.2
  • 25
    • 0034602693 scopus 로고    scopus 로고
    • Solid-state synthesis and mechanical unfolding of polymers of T4 lysozyme
    • Yang, G.L. et al. Solid-state synthesis and mechanical unfolding of polymers of T4 lysozyme. Proc. Natl. Acad. Sci. USA 97, 139-144 (2000).
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 139-144
    • Yang, G.L.1
  • 27
    • 0031011695 scopus 로고    scopus 로고
    • Reversible unfolding of individual titin immunoglobulin domains by AFM
    • Rief, M., Gautel, M., Oesterhelt, F., Fernandez, J.M. & Gaub, H.E. Reversible unfolding of individual titin immunoglobulin domains by AFM. Science 276, 1109-1112 (1997).
    • (1997) Science , vol.276 , pp. 1109-1112
    • Rief, M.1    Gautel, M.2    Oesterhelt, F.3    Fernandez, J.M.4    Gaub, H.E.5
  • 28
    • 0035852740 scopus 로고    scopus 로고
    • Forced unfolding modulated by disulfide bonds in the Ig domains of a cell adhesion molecule
    • Carl, P., Kwok, C.H., Manderson, G., Speicher, D.W. & Discher, D.E. Forced unfolding modulated by disulfide bonds in the Ig domains of a cell adhesion molecule. Proc. Natl. Acad. Sci. USA 98, 1565-1570 (2001).
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 1565-1570
    • Carl, P.1    Kwok, C.H.2    Manderson, G.3    Speicher, D.W.4    Discher, D.E.5
  • 29
    • 0036045690 scopus 로고    scopus 로고
    • Pathways and intermediates in forced unfolding of spectrin repeats
    • Altmann, S.M. et al. Pathways and intermediates in forced unfolding of spectrin repeats. Structure 10, 1085-1096 (2002).
    • (2002) Structure , vol.10 , pp. 1085-1096
    • Altmann, S.M.1
  • 30
    • 0032516205 scopus 로고    scopus 로고
    • The molecular elasticity of the extracellular matrix protein tenascin
    • Oberhauser, A.F., Marszalek, P.E., Erickson, H.P. & Fernandez, J.M. The molecular elasticity of the extracellular matrix protein tenascin. Nature 393, 181-185 (1998).
    • (1998) Nature , vol.393 , pp. 181-185
    • Oberhauser, A.F.1    Marszalek, P.E.2    Erickson, H.P.3    Fernandez, J.M.4
  • 31
    • 18344367645 scopus 로고    scopus 로고
    • Mechanical unfolding and refolding of proteins: An off-lattice model study
    • 6302, art. no.-021905
    • Li, F.Y., Yuan, J.M. & Mou, C.Y. Mechanical unfolding and refolding of proteins: an off-lattice model study. Phys. Rev. E 6302, art. no.-021905 (2001).
    • (2001) Phys. Rev. E
    • Li, F.Y.1    Yuan, J.M.2    Mou, C.Y.3
  • 32
    • 0033582763 scopus 로고    scopus 로고
    • Single molecule force spectroscopy of spectrin repeats: Low unfolding forces in helix bundles
    • Rief, M., Pascual, J., Saraste, M. & Gaub, H.E. Single molecule force spectroscopy of spectrin repeats: low unfolding forces in helix bundles. J. Mol. Biol. 286, 553-561 (1999).
    • (1999) J. Mol. Biol. , vol.286 , pp. 553-561
    • Rief, M.1    Pascual, J.2    Saraste, M.3    Gaub, H.E.4
  • 33
    • 0036343904 scopus 로고    scopus 로고
    • The protein import motor of mitochondria
    • Neupert, W. & Brunner, M. The protein import motor of mitochondria. Nat. Rev. Mol. Cell Biol. 3, 555-565 (2002).
    • (2002) Nat. Rev. Mol. Cell Biol. , vol.3 , pp. 555-565
    • Neupert, W.1    Brunner, M.2
  • 34
    • 0035266072 scopus 로고    scopus 로고
    • ATP-dependent proteases degrade their substrates by processively unraveling them from the degradation signal
    • Lee, C., Schwartz, M.P., Prakash, S., Iwakura, M. & Matouschek, A. ATP-dependent proteases degrade their substrates by processively unraveling them from the degradation signal. Mol. Cell 7, 627-637 (2001).
    • (2001) Mol. Cell , vol.7 , pp. 627-637
    • Lee, C.1    Schwartz, M.P.2    Prakash, S.3    Iwakura, M.4    Matouschek, A.5
  • 35
    • 0035282966 scopus 로고    scopus 로고
    • The mitochondrial Hsp70-dependent import system actively unfolds preproteins and shortens the lag phase of translocation
    • Lim, J.H., Martin, F., Guiard, B., Pfanner, N. & Voos, W. The mitochondrial Hsp70-dependent import system actively unfolds preproteins and shortens the lag phase of translocation. EMBO J. 20, 941-950 (2001).
    • (2001) EMBO J. , vol.20 , pp. 941-950
    • Lim, J.H.1    Martin, F.2    Guiard, B.3    Pfanner, N.4    Voos, W.5
  • 37
    • 0037099608 scopus 로고    scopus 로고
    • The protein import motor of mitochondria: A targeted molecular ratchet driving unfolding and translocation
    • Okamoto, K. et al. The protein import motor of mitochondria: a targeted molecular ratchet driving unfolding and translocation. EMBO J. 21, 3659-3671 (2002).
    • (2002) EMBO J. , vol.21 , pp. 3659-3671
    • Okamoto, K.1
  • 38
    • 0035808415 scopus 로고    scopus 로고
    • Recognition of the lipoyl domain is the ultimate determinant of substrate channelling in the pyruvate dehydrogenase multienzyme complex
    • Jones, D.D., Stott, K.M., Reche, P.A. & Perham, R.N. Recognition of the lipoyl domain is the ultimate determinant of substrate channelling in the pyruvate dehydrogenase multienzyme complex. J. Mol. Biol. 305, 49-60 (2001).
    • (2001) J. Mol. Biol. , vol.305 , pp. 49-60
    • Jones, D.D.1    Stott, K.M.2    Reche, P.A.3    Perham, R.N.4
  • 39
    • 84986512474 scopus 로고
    • Charmm - A program for macromolecular energy, minimization, and dynamics calculations
    • Brooks, B.R. et al. Charmm - a program for macromolecular energy, minimization, and dynamics calculations. J. Comput. Chem. 4, 187-217 (1983).
    • (1983) J. Comput. Chem. , vol.4 , pp. 187-217
    • Brooks, B.R.1
  • 40
    • 0033135638 scopus 로고    scopus 로고
    • Effective energy function for proteins in solution
    • Lazaridis, T. & Karplus, M. Effective energy function for proteins in solution. Proteins 35, 133-152 (1999).
    • (1999) Proteins , vol.35 , pp. 133-152
    • Lazaridis, T.1    Karplus, M.2
  • 41
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis, P.J. MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr. 24, 946-950 (1991).
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 42
    • 0028057108 scopus 로고
    • Raster3D Version 2.0 - A program for photorealistic molecular graphics
    • Merritt, E.A. & Murphy, M.E.P. Raster3D Version 2.0 - a program for photorealistic molecular graphics. Acta Crystallogr. D 50, 869-873 (1994).
    • (1994) Acta Crystallogr. D , vol.50 , pp. 869-873
    • Merritt, E.A.1    Murphy, M.E.P.2
  • 43
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure - Pattern-recognition of hydrogen-bonded and geometrical features
    • Kabsch, W. & Sander, C. Dictionary of protein secondary structure - pattern-recognition of hydrogen-bonded and geometrical features. Biopolymers 22, 2577-2637 (1983).
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.