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Volumn 90, Issue 8, 2006, Pages 2852-2866

Coiled-coil nanomechanics and uncoiling and unfolding of the superhelix and α-helices of myosin

Author keywords

[No Author keywords available]

Indexed keywords

MYOSIN; NANOPARTICLE; POLYMER;

EID: 33646172749     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1529/biophysj.105.071597     Document Type: Article
Times cited : (65)

References (57)
  • 1
    • 4344685822 scopus 로고    scopus 로고
    • Scaffolds, levers, rods and springs: Diverse cellular functions of long coiled-coil proteins
    • Rose, A., and I. Meier. 2004. Scaffolds, levers, rods and springs: diverse cellular functions of long coiled-coil proteins. Cell. Mol. Life Sci. 61:1996-2009.
    • (2004) Cell. Mol. Life Sci. , vol.61 , pp. 1996-2009
    • Rose, A.1    Meier, I.2
  • 2
    • 0039529834 scopus 로고
    • Studies on the tryptic digestion of myosin
    • Mihalyi, E., and W. F. Harrington. 1959. Studies on the tryptic digestion of myosin. Biochim. Biophys. Acta. 36:447-466.
    • (1959) Biochim. Biophys. Acta , vol.36 , pp. 447-466
    • Mihalyi, E.1    Harrington, W.F.2
  • 3
    • 0022419381 scopus 로고
    • Negative staining of myosin molecules
    • Walker, M., P. Knight, and J. Trinick. 1985. Negative staining of myosin molecules. J. Mol. Biol. 184:535-542.
    • (1985) J. Mol. Biol. , vol.184 , pp. 535-542
    • Walker, M.1    Knight, P.2    Trinick, J.3
  • 4
    • 12844288158 scopus 로고    scopus 로고
    • High flexibility of the actomyosin crossbridge resides in skeletal muscle myosin subfragment-2 as demonstrated by a new single molecule assay
    • Gundapaneni, D., J. Xu, and D. D. Root. 2005. High flexibility of the actomyosin crossbridge resides in skeletal muscle myosin subfragment-2 as demonstrated by a new single molecule assay. J. Struct. Biol. 149:117-126.
    • (2005) J. Struct. Biol. , vol.149 , pp. 117-126
    • Gundapaneni, D.1    Xu, J.2    Root, D.D.3
  • 5
    • 0004161470 scopus 로고    scopus 로고
    • Oxford University Press, New York
    • Sellers, J. R. 1999. Myosins. Oxford University Press, New York.
    • (1999) Myosins
    • Sellers, J.R.1
  • 7
    • 0015236610 scopus 로고
    • Proposed mechanism of force generation in striated muscle
    • Huxley, A. F., and R. M. Simmons. 1971. Proposed mechanism of force generation in striated muscle. Nature. 233:533-538.
    • (1971) Nature , vol.233 , pp. 533-538
    • Huxley, A.F.1    Simmons, R.M.2
  • 10
    • 1642417250 scopus 로고    scopus 로고
    • The dance of actin and myosin: A structural and spectroscopic perspective
    • Root, D. D. 2002. The dance of actin and myosin: a structural and spectroscopic perspective. Cell Biochem. Biophys. 37:111-139.
    • (2002) Cell Biochem. Biophys. , vol.37 , pp. 111-139
    • Root, D.D.1
  • 11
    • 11144241933 scopus 로고    scopus 로고
    • Actomyosin systems of biological motility
    • Levitsky, D. I. 2004. Actomyosin systems of biological motility. Biochemistry (Mosc.). 69:1177-1189.
    • (2004) Biochemistry (Mosc.) , vol.69 , pp. 1177-1189
    • Levitsky, D.I.1
  • 15
    • 11144225866 scopus 로고    scopus 로고
    • Rod mutations associated with MYH9-related disorders disrupt nonmuscle myosin-IIA assembly
    • Franke, J. D., F. Dong, W. L. Rickoll, M. J. Kelley, and D. P. Kiehart. 2005. Rod mutations associated with MYH9-related disorders disrupt nonmuscle myosin-IIA assembly. Blood. 105:161-169.
    • (2005) Blood , vol.105 , pp. 161-169
    • Franke, J.D.1    Dong, F.2    Rickoll, W.L.3    Kelley, M.J.4    Kiehart, D.P.5
  • 19
    • 0034029857 scopus 로고    scopus 로고
    • A critical review of the structural mechanics of wool and hair fibres
    • Hearle, J. W. S. 2000. A critical review of the structural mechanics of wool and hair fibres. Int. J. Biol. Macromol. 27:123-138.
    • (2000) Int. J. Biol. Macromol. , vol.27 , pp. 123-138
    • Hearle, J.W.S.1
  • 20
    • 0036977558 scopus 로고    scopus 로고
    • The myosin coiled-coil is a truly elastic protein structure
    • Schwaiger, I., C. Sattler, D. R. Hostetter, and M. Rief. 2002. The myosin coiled-coil is a truly elastic protein structure. Nat. Mater. 1:232-235.
    • (2002) Nat. Mater. , vol.1 , pp. 232-235
    • Schwaiger, I.1    Sattler, C.2    Hostetter, D.R.3    Rief, M.4
  • 21
    • 0034895411 scopus 로고    scopus 로고
    • Single molecule measurements of titin elasticity
    • Wang, K., J. G. Forbes, and A. J. Jin. 2001. Single molecule measurements of titin elasticity. Prog. Biophys. Mol. Biol. 77:1-44.
    • (2001) Prog. Biophys. Mol. Biol. , vol.77 , pp. 1-44
    • Wang, K.1    Forbes, J.G.2    Jin, A.J.3
  • 22
    • 0014952464 scopus 로고
    • Self-association in the myosin system at high ionic strength. I. Sensitivity of the interaction to pH and ionic environment
    • Godfrey, J., E., and W. Harrington, F. 1970. Self-association in the myosin system at high ionic strength. I. Sensitivity of the interaction to pH and ionic environment. Biochemistry 9:886-893.
    • (1970) Biochemistry , vol.9 , pp. 886-893
    • Godfrey, J.E.1    W Harrington, F.2
  • 23
    • 0023667713 scopus 로고
    • Hinging of rabbit myosin rod
    • Rodgers, M. E., and W. F. Harrington. 1987. Hinging of rabbit myosin rod. Biochemistry. 26:8697-8703.
    • (1987) Biochemistry , vol.26 , pp. 8697-8703
    • Rodgers, M.E.1    Harrington, W.F.2
  • 24
    • 0021714910 scopus 로고
    • The purification of myosin long subfragment-2 by DEAE-Sepharose Cl-6b ion-exchange chromatography
    • Borras-Cuesta, F., and E. Truche. 1984. The purification of myosin long subfragment-2 by DEAE-Sepharose Cl-6b ion-exchange chromatography. Anal. Biochem. 142:84-87.
    • (1984) Anal. Biochem. , vol.142 , pp. 84-87
    • Borras-Cuesta, F.1    Truche, E.2
  • 25
    • 0017336444 scopus 로고
    • Studies on chymotryptic digestion of myosin: Effects of divalent-cations on proteolytic susceptibility
    • Weeds, A. G., and B. Pope. 1977. Studies on chymotryptic digestion of myosin: effects of divalent-cations on proteolytic susceptibility. J. Mol. Biol. 111:129-157.
    • (1977) J. Mol. Biol. , vol.111 , pp. 129-157
    • Weeds, A.G.1    Pope, B.2
  • 26
    • 0024448151 scopus 로고
    • Calculation of protein extinction coefficients from amino acid sequence data
    • Gill, S. C., and P. H. von Hippel. 1989. Calculation of protein extinction coefficients from amino acid sequence data. Anal. Biochem. 182:319-326.
    • (1989) Anal. Biochem. , vol.182 , pp. 319-326
    • Gill, S.C.1    Von Hippel, P.H.2
  • 27
    • 36449007442 scopus 로고
    • Calibration of atomic-force microscope tips
    • Hutter, J. L., and J. Bechhoefer. 1993. Calibration of atomic-force microscope tips. Rev. Sci. Instrum. 64:1868-1873.
    • (1993) Rev. Sci. Instrum. , vol.64 , pp. 1868-1873
    • Hutter, J.L.1    Bechhoefer, J.2
  • 28
    • 0028071373 scopus 로고
    • Entropic elasticity of lambda-phage DNA
    • Bustamante, C., J. F. Marko, E. D. Siggia, and S. Smith. 1994. Entropic elasticity of lambda-phage DNA. Science. 265:1599-1600.
    • (1994) Science , vol.265 , pp. 1599-1600
    • Bustamante, C.1    Marko, J.F.2    Siggia, E.D.3    Smith, S.4
  • 30
    • 0032851597 scopus 로고    scopus 로고
    • Determination of fluorescent probe orientations on biomolecules by conformational searching: Algorithm testing and applications to the atomic model of myosin
    • Root, D. D., S. G. Xin, X. Jin, and M. A. McAllister. 1999. Determination of fluorescent probe orientations on biomolecules by conformational searching: algorithm testing and applications to the atomic model of myosin. J. Struct. Biol. 127:22-34.
    • (1999) J. Struct. Biol. , vol.127 , pp. 22-34
    • Root, D.D.1    Xin, S.G.2    Jin, X.3    McAllister, M.A.4
  • 31
    • 1542297704 scopus 로고    scopus 로고
    • Binding of calcium ions to an avian flight muscle troponin T
    • Zhang, Z. L., J. P. Jin, and D. D. Root. 2004. Binding of calcium ions to an avian flight muscle troponin T. Biochemistry. 43:2645-2655.
    • (2004) Biochemistry , vol.43 , pp. 2645-2655
    • Zhang, Z.L.1    Jin, J.P.2    Root, D.D.3
  • 32
    • 21444449052 scopus 로고    scopus 로고
    • Stretching globular polymers. I. Single chains
    • Craig, A., and E. M. Terentjev. 2005. Stretching globular polymers. I. Single chains. J. Chem. Phys. 122:194901.
    • (2005) J. Chem. Phys. , vol.122 , pp. 194901
    • Craig, A.1    Terentjev, E.M.2
  • 35
    • 14844297706 scopus 로고    scopus 로고
    • The elasticity of individual titin PEVK exons measured by single molecule atomic force microscopy
    • Sarkar, A., S. Caamano, and J. M. Fernandez. 2005. The elasticity of individual titin PEVK exons measured by single molecule atomic force microscopy. J. Biol. Chem. 280:6261-6264.
    • (2005) J. Biol. Chem. , vol.280 , pp. 6261-6264
    • Sarkar, A.1    Caamano, S.2    Fernandez, J.M.3
  • 38
    • 4344586794 scopus 로고    scopus 로고
    • Simultaneous dynamic stiffness and extension profiles of single titin molecules: Nanomechanical evidence for unfolding intermediates
    • Forbes, J. G., and K. Wang. 2004. Simultaneous dynamic stiffness and extension profiles of single titin molecules: nanomechanical evidence for unfolding intermediates. J. Vac. Sci. Technol. A. 22:1439-1443.
    • (2004) J. Vac. Sci. Technol. A , vol.22 , pp. 1439-1443
    • Forbes, J.G.1    Wang, K.2
  • 40
    • 84982060514 scopus 로고
    • Rontgenuntersuchung Geloster Fadenmolekule
    • Kratky, O., and G. Porod. 1949. Rontgenuntersuchung Geloster Fadenmolekule. [in German.] Recl. Trav. Chim. Pay. B. 68:1106-1122.
    • (1949) Recl. Trav. Chim. Pay. B , vol.68 , pp. 1106-1122
    • Kratky, O.1    Porod, G.2
  • 42
    • 0004097995 scopus 로고
    • J. B. Sykes and W. H. Reid, translator. Butterworth-Heinemann, Oxford, UK
    • Landau, L. D., and E. M. Lifshitz. 1986. Theory of Elasticity. J. B. Sykes and W. H. Reid, translator. Butterworth-Heinemann, Oxford, UK.
    • (1986) Theory of Elasticity
    • Landau, L.D.1    Lifshitz, E.M.2
  • 44
    • 0031848099 scopus 로고    scopus 로고
    • Unfolding of titin immunoglobulin domains by steered molecular dynamics simulation
    • Lu, H., B. Isralewitz, A. Krammer, V. Vogel, and K. Schulten. 1998. Unfolding of titin immunoglobulin domains by steered molecular dynamics simulation. Biophys. J. 75:662-671.
    • (1998) Biophys. J. , vol.75 , pp. 662-671
    • Lu, H.1    Isralewitz, B.2    Krammer, A.3    Vogel, V.4    Schulten, K.5
  • 45
    • 0033064934 scopus 로고    scopus 로고
    • Unraveling proteins: A molecular mechanics study
    • Rohs, R., C. Etchebest, and R. Lavery. 1999. Unraveling proteins: a molecular mechanics study. Biophys. J. 76:2760-2768.
    • (1999) Biophys. J. , vol.76 , pp. 2760-2768
    • Rohs, R.1    Etchebest, C.2    Lavery, R.3
  • 46
    • 0034491563 scopus 로고    scopus 로고
    • Spring mechanics of alpha-helical polypeptide
    • Idiris, A., M. T. Alam, and A. Ikai. 2000. Spring mechanics of alpha-helical polypeptide. Protein Eng. 13:763-770.
    • (2000) Protein Eng. , vol.13 , pp. 763-770
    • Idiris, A.1    Alam, M.T.2    Ikai, A.3
  • 47
    • 0035883960 scopus 로고    scopus 로고
    • Modified atomic force microscope applied to the measurement of elastic modulus for a single peptide molecule
    • Ptak, A., S. Takeda, C. Nakamura, J. Miyake, M. Kageshima, S. P. Jarvis, and H. Tokumoto. 2001. Modified atomic force microscope applied to the measurement of elastic modulus for a single peptide molecule. J. Appl. Phys. 90:3095-3099.
    • (2001) J. Appl. Phys. , vol.90 , pp. 3095-3099
    • Ptak, A.1    Takeda, S.2    Nakamura, C.3    Miyake, J.4    Kageshima, M.5    Jarvis, S.P.6    Tokumoto, H.7
  • 48
    • 0037187212 scopus 로고    scopus 로고
    • Molecular dynamics study of mechanical extension of polyalanine by AFM cantilever
    • Masugata, K., A. Ikai, and S. Okazaki. 2002. Molecular dynamics study of mechanical extension of polyalanine by AFM cantilever. Appl. Surf. Sci. 188:372-376.
    • (2002) Appl. Surf. Sci. , vol.188 , pp. 372-376
    • Masugata, K.1    Ikai, A.2    Okazaki, S.3
  • 50
    • 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
  • 51
    • 0034653908 scopus 로고    scopus 로고
    • The coiled-coil trigger site of the rod domain of cortexillin I unveils a distinct network of interhelical and intrahelical salt bridges
    • Burkhard, P., R. A. Kammerer, M. O. Steinmetz, G. P. Bourenkov, and U. Aebi. 2000. The coiled-coil trigger site of the rod domain of cortexillin I unveils a distinct network of interhelical and intrahelical salt bridges. Structure. 8:223-230.
    • (2000) Structure , vol.8 , pp. 223-230
    • Burkhard, P.1    Kammerer, R.A.2    Steinmetz, M.O.3    Bourenkov, G.P.4    Aebi, U.5
  • 52
    • 20544465799 scopus 로고    scopus 로고
    • Mechanical unfolding of TNfn3: The unfolding pathway of a fnIII domain probed by protein engineering, AFM and MD simulation
    • Ng, S. P., R. W. S. Rounsevell, A. Steward, C. D. Geierhaas, P. M. Williams, E. Paci, and J. Clarke. 2005. Mechanical unfolding of TNfn3: the unfolding pathway of a fnIII domain probed by protein engineering, AFM and MD simulation. J. Mol. Biol. 350:776-789.
    • (2005) J. Mol. Biol. , vol.350 , 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
  • 53
    • 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
  • 55
    • 0029075829 scopus 로고
    • Unbinding force of a single motor molecule of muscle measured using optical tweezers
    • Nishizaka, T., H. Miyata, H. Yoshikawa, S. Ishiwata, and K. Kinosita. 1995. Unbinding force of a single motor molecule of muscle measured using optical tweezers. Nature. 377:251-254.
    • (1995) Nature , vol.377 , pp. 251-254
    • Nishizaka, T.1    Miyata, H.2    Yoshikawa, H.3    Ishiwata, S.4    Kinosita, K.5
  • 56
    • 0030992359 scopus 로고    scopus 로고
    • Scanning force microscopy of the interaction events between a single molecule of heavy meromyosin and actin
    • Nakajima, H., Y. Kunioka, K. Nakano, K. Shimizu, M. Seto, and T. Ando. 1997. Scanning force microscopy of the interaction events between a single molecule of heavy meromyosin and actin. Biochem. Biophys. Res. Commun. 234:178-182.
    • (1997) Biochem. Biophys. Res. Commun. , vol.234 , pp. 178-182
    • Nakajima, H.1    Kunioka, Y.2    Nakano, K.3    Shimizu, K.4    Seto, M.5    Ando, T.6


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