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Volumn 99, Issue 1, 2010, Pages 257-262

Dynamics of the coiled-coil unfolding transition of myosin rod probed by dissipation force spectrum

Author keywords

[No Author keywords available]

Indexed keywords

MYOSIN SUBFRAGMENT;

EID: 77954358608     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1016/j.bpj.2010.04.007     Document Type: Article
Times cited : (20)

References (25)
  • 1
    • 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
  • 2
    • 0028081494 scopus 로고
    • X-ray diffraction evidence for the extensibility of actin and myosin filaments during muscle contraction
    • Wakabayashi, K., Y. Sugimoto,..., Y. Amemiya. 1994. X-ray diffraction evidence for the extensibility of actin and myosin filaments during muscle contraction, Biophys. J. 67:2422-2435.
    • (1994) Biophys. J. , vol.67 , pp. 2422-2435
    • Wakabayashi, K.1    Sugimoto, Y.2    Amemiya, Y.3
  • 3
    • 0028081493 scopus 로고
    • X-ray diffraction measurements of the extensibility of actin and myosin filaments in contracting muscle
    • Huxley, H. E., A. Stewart,..., T. Irving. 1994. X-ray diffraction measurements of the extensibility of actin and myosin filaments in contracting muscle. Biophys. J. 67:2411-2421.
    • (1994) Biophys. J. , vol.67 , pp. 2411-2421
    • Huxley, H.E.1    Stewart, A.2    Irving, T.3
  • 4
    • 0027189534 scopus 로고
    • Viscoelasticity of the sarcomere matrix of skeletal muscles. The titin-myosin composite filament is a dual-stage molecular spring
    • Wang, K., R. McCarter,..., R. Ramirez-Mitchell. 1993. Viscoelasticity of the sarcomere matrix of skeletal muscles. The titin-myosin composite filament is a dual-stage molecular spring. Biophys. J. 64:1161-1177.
    • (1993) Biophys. J. , vol.64 , pp. 1161-1177
    • Wang, K.1    McCarter, R.2    Ramirez-Mitchell, R.3
  • 5
    • 0035115798 scopus 로고    scopus 로고
    • Unfolding of titin domains explains the viscoelastic behavior of skeletal myofibrils
    • Minajeva, A., M. Kulke, ..., W. A. Linke. 2001. Unfolding of titin domains explains the viscoelastic behavior of skeletal myofibrils. Biophys. J. 80:1442-1451.
    • (2001) Biophys. J. , vol.80 , pp. 1442-1451
    • Minajeva, A.1    Kulke, M.2    Linke, W.A.3
  • 6
    • 0029850038 scopus 로고    scopus 로고
    • Viscoelasticity and function of connectin/titin filaments in skinned muscle fibers
    • Higuchi, H. 1996. Viscoelasticity and function of connectin/titin filaments in skinned muscle fibers. Adv. Biophys. 33:159-171.
    • (1996) Adv. Biophys. , vol.33 , pp. 159-171
    • Higuchi, H.1
  • 7
    • 23044507613 scopus 로고    scopus 로고
    • Paramyosin phosphorylation site disruption affects indirect flight muscle stiffness and power generation in Drosophila melanogaster
    • Liu, H., M. S. Miller, ..., S. I. Bernstein. 2005. Paramyosin phosphorylation site disruption affects indirect flight muscle stiffness and power generation in Drosophila melanogaster. Proc. Natl. Acad. Sci. USA. 102:10522-10527.
    • (2005) Proc. Natl. Acad. Sci. USA. , vol.102 , pp. 10522-10527
    • Liu, H.1    Miller, M.S.2    Bernstein, S.I.3
  • 8
    • 0020485885 scopus 로고
    • Flexibility of myosin rod determined from, dilute solution viscoelastic measurements
    • Hvidt, S., F. H. Nestler,..., J. D. Ferry. 1982. Flexibility of myosin rod determined from, dilute solution viscoelastic measurements. Biochemistry. 21:4064-4073.
    • (1982) Biochemistry. , vol.21 , pp. 4064-4073
    • Hvidt, S.1    Nestler, F.H.2    Ferry, J.D.3
  • 9
    • 0036977558 scopus 로고    scopus 로고
    • The myosin coiled-coil is a truly elastic protein structure
    • Schwaiger, I., C. Sattler,..., 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    Rief, M.3
  • 10
    • 33646172749 scopus 로고    scopus 로고
    • Coiled-coil nanomechanies and uncoiling and unfolding of the superhelix and a-helices of myosin
    • Root, D. D., V. K. Yadavalli,..., K. Wang. 2006. Coiled-coil nanomechanies and uncoiling and unfolding of the superhelix and a-helices of myosin. Biophys. J. 90:2852-2866.
    • (2006) Biophys. J. , vol.90 , pp. 2852-2866
    • Root, D.D.1    Yadavalli, V.K.2    Wang, K.3
  • 11
    • 6444225109 scopus 로고    scopus 로고
    • Viscoelastic properties of single polysaccharide molecules determined by analysis of thermally driven oscillations of an atomic force microscope cantilever
    • Kawakami, M., K. Byrne,..., D. A. Smith. 2004. Viscoelastic properties of single polysaccharide molecules determined by analysis of thermally driven oscillations of an atomic force microscope cantilever. Langmuir. 20:9299-9303.
    • (2004) Langmuir. , vol.20 , pp. 9299-9303
    • Kawakami, M.1    Byrne, K.2    Smith, D.A.3
  • 12
    • 0034300937 scopus 로고    scopus 로고
    • Active quality factor control in liquids for force spectroscopy
    • Humphris, A. D. L., J. Tamayo, and M. J. Miles. 2000. Active quality factor control in liquids for force spectroscopy. Langmuir. 16:7891-7894.
    • (2000) Langmuir. , vol.16 , pp. 7891-7894
    • Humphris, A.D.L.1    Tamayo, J.2    Miles, M.J.3
  • 13
    • 18844446972 scopus 로고    scopus 로고
    • Viscoelastic measurements of single molecules on a millisecond time scale by magnetically driven oscillation of an atomic force microscope cantilever
    • Kawakami, M., K. Byrne,..., D. A. Smith. 2005. Viscoelastic measurements of single molecules on a millisecond time scale by magnetically driven oscillation of an atomic force microscope cantilever. Langmuir. 21:4765-4772.
    • (2005) Langmuir. , vol.21 , pp. 4765-4772
    • Kawakami, M.1    Byrne, K.2    Smith, D.A.3
  • 14
    • 33745686052 scopus 로고    scopus 로고
    • Viscoelastic study of the mechanical unfolding of a protein by AFM
    • Kawakami, M., K. Byrne, ..., D. A. Smith, 2006. Viscoelastic study of the mechanical unfolding of a protein by AFM. Biophys. J. 91: L16-L18.
    • (2006) Biophys. J. , vol.91
    • Kawakami, M.1    Byrne, K.2    Smith, D.A.3
  • 15
    • 33748138544 scopus 로고    scopus 로고
    • Viscoelastic properties of single poly(ethylene glycol) molecules
    • Kawakami, M., K. Byrne, ..., D. A. Smith. 2006. Viscoelastic properties of single poly(ethylene glycol) molecules. ChemPhysChem. 7:1710-1716.
    • (2006) ChemPhysChem. , vol.7 , pp. 1710-1716
    • Kawakami, M.1    Byrne, K.2    Smith, D.A.3
  • 16
    • 50849135501 scopus 로고    scopus 로고
    • Internal friction of single polypeptide chains at high, stretch
    • Khatri, B. S., K. Byrne,..., T. C. McLeish. 2008. Internal friction of single polypeptide chains at high, stretch. Faraday Discuss. 139: 35-51.
    • (2008) Faraday Discuss. , vol.139 , pp. 35-51
    • Khatri, B.S.1    Byrne, K.2    McLeish, T.C.3
  • 17
    • 33947700979 scopus 로고    scopus 로고
    • Entropy and barrier-controlled fluctuations determine conformational viscoelasticity of single biomolecules
    • Khatri, B. S., M. Kawakami,..., T. C. McLeish. 2007. Entropy and barrier-controlled fluctuations determine conformational viscoelasticity of single biomolecules. Biophys. J. 92:1825-1835.
    • (2007) Biophys. J. , vol.92 , pp. 1825-1835
    • Khatri, B.S.1    Kawakami, M.2    McLeish, T.C.3
  • 18
    • 0036280490 scopus 로고    scopus 로고
    • The effect of core destabilization on the mechanical resistance of I27
    • Brockwell, D. J., G. S. Beddard,..., S. E. Radford. 2002. The effect of core destabilization on the mechanical resistance of I27. Biophys. J. 83:458-472.
    • (2002) Biophys. J. , vol.83 , pp. 458-472
    • Brockwell, D.J.1    Beddard, G.S.2    Radford, S.E.3
  • 19
    • 0036891724 scopus 로고    scopus 로고
    • Mechanically unfolding proteins: The effect of unfolding history and the supramolecular scaffold
    • Zinober, R. C. D. J. Brockwell,..., D. A. Smith. 2002. Mechanically unfolding proteins: the effect of unfolding history and the supramolecular scaffold. Protein Sci. 11:2759-2765.
    • (2002) Protein Sci. , vol.11 , pp. 2759-2765
    • Zinober, R.C.1    Brockwell, D.J.2    Smith, D.A.3
  • 20
    • 58149356274 scopus 로고    scopus 로고
    • The effect of temperature on mechanical resistance of the native and intermediate states of 127
    • Taniguchi, Y., D. J. Brockwell, and M. Kawakami. 2008. The effect of temperature on mechanical resistance of the native and intermediate states of 127. Biophys. J. 95:5296-5305.
    • (2008) Biophys. J. , vol.95 , pp. 5296-5305
    • Taniguchi, Y.1    Brockwell, D.J.2    Kawakami, M.3
  • 22
    • 0029075829 scopus 로고
    • Unbinding force of a single motor molecule of muscle measured using optical tweezers
    • Nishizaka, T., H. Miyata,..., K. Kinosita, Jr. 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    Kinosita Jr., K.3
  • 23
    • 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, ..., 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    Ando, T.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.