메뉴 건너뛰기




Volumn 170, Issue 2, 2010, Pages 313-318

The relationship between curvature, flexibility and persistence length in the tropomyosin coiled-coil

Author keywords

Actin; Coiled coils; Molecular Dynamics; Persistence length; Thin filaments; Tropomyosin

Indexed keywords

F ACTIN; TROPOMYOSIN;

EID: 77951977112     PISSN: 10478477     EISSN: 10958657     Source Type: Journal    
DOI: 10.1016/j.jsb.2010.01.016     Document Type: Article
Times cited : (71)

References (35)
  • 1
    • 0029618936 scopus 로고
    • Determination of DNA persistence length by cryo-electron microscopy. Separation of the static and dynamic contributions to the apparent persistence length of DNA
    • Bednar J., Furrer P., Katritch V., Stasiak A.Z., Dubochet J., Stasiak A. Determination of DNA persistence length by cryo-electron microscopy. Separation of the static and dynamic contributions to the apparent persistence length of DNA. J. Mol. Biol. 1995, 254:579-594.
    • (1995) J. Mol. Biol. , vol.254 , pp. 579-594
    • Bednar, J.1    Furrer, P.2    Katritch, V.3    Stasiak, A.Z.4    Dubochet, J.5    Stasiak, A.6
  • 2
    • 84985648233 scopus 로고
    • Microscopic persistence length of native DNA: its relation to average molecular dimensions
    • Bettini A., Pozzan M.R., Valdevit E., Frontali C. Microscopic persistence length of native DNA: its relation to average molecular dimensions. Biopolymers 1980, 19:1689-1694.
    • (1980) Biopolymers , vol.19 , pp. 1689-1694
    • Bettini, A.1    Pozzan, M.R.2    Valdevit, E.3    Frontali, C.4
  • 3
    • 0004150063 scopus 로고    scopus 로고
    • Cambridge University Press, Cambridge, UK
    • Boal D.H. Mechanics of the Cell 2002, Cambridge University Press, Cambridge, UK.
    • (2002) Mechanics of the Cell
    • Boal, D.H.1
  • 8
    • 0034127611 scopus 로고    scopus 로고
    • Analysis of the three-dimensional trajectories of organisms: estimates for the velocity, curvature and torsion from positional information
    • Crenshaw H.C., Ciampaglio C.N., McHenry M. Analysis of the three-dimensional trajectories of organisms: estimates for the velocity, curvature and torsion from positional information. J. Exp. Biol. 2000, 203:961-982.
    • (2000) J. Exp. Biol. , vol.203 , pp. 961-982
    • Crenshaw, H.C.1    Ciampaglio, C.N.2    McHenry, M.3
  • 10
    • 0018488093 scopus 로고
    • An absolute method for the determination of the persistence length of native DNA from electron micrographs
    • Frontali C., Dore E., Ferrrauto A., Gratton E., Bettini A., Pozzan M.R., Valdevit E. An absolute method for the determination of the persistence length of native DNA from electron micrographs. Biopolymers 1979, 18:1353-1373.
    • (1979) Biopolymers , vol.18 , pp. 1353-1373
    • Frontali, C.1    Dore, E.2    Ferrrauto, A.3    Gratton, E.4    Bettini, A.5    Pozzan, M.R.6    Valdevit, E.7
  • 11
    • 0036193163 scopus 로고    scopus 로고
    • Modeling thin filament cooperativity
    • Geeves M.A., Lehrer S.S. Modeling thin filament cooperativity. Biophys. J. 2002, 82:1677-1681.
    • (2002) Biophys. J. , vol.82 , pp. 1677-1681
    • Geeves, M.A.1    Lehrer, S.S.2
  • 12
    • 62449145371 scopus 로고    scopus 로고
    • Gestalt-binding of tropomyosin to actin filaments
    • Holmes K.C., Lehman W. Gestalt-binding of tropomyosin to actin filaments. J. Muscle Res. Cell Motil. 2008, 29:213-219.
    • (2008) J. Muscle Res. Cell Motil. , vol.29 , pp. 213-219
    • Holmes, K.C.1    Lehman, W.2
  • 13
    • 0008359705 scopus 로고
    • Flexibility of light meromyosin and other coiled-coil α-helical proteins
    • Hvidt S., Ferry J.D., Roelke D.L., Greaser M.L. Flexibility of light meromyosin and other coiled-coil α-helical proteins. Macromolecules 1983, 16:740-745.
    • (1983) Macromolecules , vol.16 , pp. 740-745
    • Hvidt, S.1    Ferry, J.D.2    Roelke, D.L.3    Greaser, M.L.4
  • 15
    • 73149102752 scopus 로고    scopus 로고
    • The shape and flexibility of tropomyosin coiled-coils: implications for actin filament assembly and regulation
    • Li X., Holmes K.C., Lehman W., Jung H., Fischer S. The shape and flexibility of tropomyosin coiled-coils: implications for actin filament assembly and regulation. J. Mol. Biol. 2010, 395:327-339.
    • (2010) J. Mol. Biol. , vol.395 , pp. 327-339
    • Li, X.1    Holmes, K.C.2    Lehman, W.3    Jung, H.4    Fischer, S.5
  • 16
    • 0028940312 scopus 로고
    • An atomic model of the unregulated thin filament obtained by X-ray fiber diffraction on oriented actin-tropomyosin gels
    • Lorenz M., Poole K.J.V., Popp D., Rosenbaum G., Holmes K.C. An atomic model of the unregulated thin filament obtained by X-ray fiber diffraction on oriented actin-tropomyosin gels. J. Mol. Biol. 1995, 246:108-119.
    • (1995) J. Mol. Biol. , vol.246 , pp. 108-119
    • Lorenz, M.1    Poole, K.J.V.2    Popp, D.3    Rosenbaum, G.4    Holmes, K.C.5
  • 17
    • 0027234056 scopus 로고
    • Regulation of the interaction between actin and myosin subfragment 1: evidence for three states of the thin filament
    • McKillop D., Geeves M. Regulation of the interaction between actin and myosin subfragment 1: evidence for three states of the thin filament. Biophys. J. 1993, 65:693-701.
    • (1993) Biophys. J. , vol.65 , pp. 693-701
    • McKillop, D.1    Geeves, M.2
  • 19
    • 0019075125 scopus 로고
    • Motions of tropomyosin: crystal as metaphor
    • Phillips G.N., Fillers J.P., Cohen C. Motions of tropomyosin: crystal as metaphor. Biophys. J. 1980, 32:485.
    • (1980) Biophys. J. , vol.32 , pp. 485
    • Phillips, G.N.1    Fillers, J.P.2    Cohen, C.3
  • 20
    • 0030021059 scopus 로고    scopus 로고
    • Mechanical properties of tropomyosin and implications for muscle regulation
    • Phillips G.N., Chacko S. Mechanical properties of tropomyosin and implications for muscle regulation. Biopolymers 1996, 38:89-95.
    • (1996) Biopolymers , vol.38 , pp. 89-95
    • Phillips, G.N.1    Chacko, S.2
  • 21
    • 33747767574 scopus 로고    scopus 로고
    • A comparison of muscle thin filament models obtained from electron microscopy reconstructions and low-angle X-ray fibre diagrams from non-overlap muscle
    • Poole K.J., Lorenz M., Evans G., Rosenbaum G., Pirani A., Craig R., Tobacman L.S., Lehman W., Holmes K.C. A comparison of muscle thin filament models obtained from electron microscopy reconstructions and low-angle X-ray fibre diagrams from non-overlap muscle. J. Struct. Biol. 2006, 155:273-284.
    • (2006) J. Struct. Biol. , vol.155 , pp. 273-284
    • Poole, K.J.1    Lorenz, M.2    Evans, G.3    Rosenbaum, G.4    Pirani, A.5    Craig, R.6    Tobacman, L.S.7    Lehman, W.8    Holmes, K.C.9
  • 22
    • 33845365528 scopus 로고    scopus 로고
    • A computational study of nucleosomal DNA flexibility
    • Ruscio J.Z., Onufriev A. A computational study of nucleosomal DNA flexibility. Biophys. J. 2006, 91:4121-4132.
    • (2006) Biophys. J. , vol.91 , pp. 4121-4132
    • Ruscio, J.Z.1    Onufriev, A.2
  • 23
    • 0029026516 scopus 로고
    • Static contributions to the persistence length of DNA and dynamic contributions to DNA curvature
    • Schellmann J.A., Harvey S.C. Static contributions to the persistence length of DNA and dynamic contributions to DNA curvature. Biophys. Chem. 1995, 55:95-114.
    • (1995) Biophys. Chem. , vol.55 , pp. 95-114
    • Schellmann, J.A.1    Harvey, S.C.2
  • 24
    • 0021646425 scopus 로고
    • 2+-activation of striated muscle contraction
    • 2+-activation of striated muscle contraction. Biophys. J. 1984, 46:541-543.
    • (1984) Biophys. J. , vol.46 , pp. 541-543
    • Shiner, J.1    Solaro, R.2
  • 25
    • 0344198181 scopus 로고    scopus 로고
    • Local destabilization of the tropomyosin coiled coil gives the molecular flexibility required for actin binding
    • Singh A., Hitchcock-DeGregori S.E. Local destabilization of the tropomyosin coiled coil gives the molecular flexibility required for actin binding. Biochemistry 2003, 42:14114-14121.
    • (2003) Biochemistry , vol.42 , pp. 14114-14121
    • Singh, A.1    Hitchcock-DeGregori, S.E.2
  • 26
    • 33644795360 scopus 로고    scopus 로고
    • Dual requirement for flexibility and specificity for binding of the coiled-coil tropomyosin to its target, actin
    • Singh A., Hitchcock-DeGregori S.E. Dual requirement for flexibility and specificity for binding of the coiled-coil tropomyosin to its target, actin. Structure 2006, 14:43-50.
    • (2006) Structure , vol.14 , pp. 43-50
    • Singh, A.1    Hitchcock-DeGregori, S.E.2
  • 28
    • 0036445512 scopus 로고    scopus 로고
    • Analysis of α-helical coiled coils with the program TWISTER reveals a structure mechanism for stutter compensation
    • Strelkov S.V., Burkhard P. Analysis of α-helical coiled coils with the program TWISTER reveals a structure mechanism for stutter compensation. J. Struct. Biol. 2002, 137:54-64.
    • (2002) J. Struct. Biol. , vol.137 , pp. 54-64
    • Strelkov, S.V.1    Burkhard, P.2
  • 29
    • 43749096824 scopus 로고    scopus 로고
    • Conserved ASP 137 imparts flexibility to tropomyosin and affects function
    • Sumida J.P., Wu E., Lehrer S.S. Conserved ASP 137 imparts flexibility to tropomyosin and affects function. J. Biol. Chem. 2008, 283:6728-6734.
    • (2008) J. Biol. Chem. , vol.283 , pp. 6728-6734
    • Sumida, J.P.1    Wu, E.2    Lehrer, S.S.3
  • 30
    • 0024511304 scopus 로고
    • Flexibility of smooth and skeletal tropomyosins
    • Swenson C.A., Stellwagen N.C. Flexibility of smooth and skeletal tropomyosins. Biopolymers 1989, 28:955-963.
    • (1989) Biopolymers , vol.28 , pp. 955-963
    • Swenson, C.A.1    Stellwagen, N.C.2
  • 31
    • 0030004861 scopus 로고    scopus 로고
    • Thin filament-mediated regulation of cardiac contraction
    • Tobacman L.S. Thin filament-mediated regulation of cardiac contraction. Annu. Rev. Physiol. 1996, 58:447-481.
    • (1996) Annu. Rev. Physiol. , vol.58 , pp. 447-481
    • Tobacman, L.S.1
  • 32
    • 0001498045 scopus 로고
    • Static persistence length of DNA
    • Adenine Press, Albany, NY, W.K. Olson, M.H. Sarma, R.H. Sarma, M.S. Sundaralinjam (Eds.)
    • Trifonov E.N., Tan R.K.Z., Harvey S.C. Static persistence length of DNA. Structure and Expression 1988, 243-254. Adenine Press, Albany, NY. W.K. Olson, M.H. Sarma, R.H. Sarma, M.S. Sundaralinjam (Eds.).
    • (1988) Structure and Expression , pp. 243-254
    • Trifonov, E.N.1    Tan, R.K.Z.2    Harvey, S.C.3
  • 33
    • 0031566964 scopus 로고    scopus 로고
    • Steric-model for activation of muscle thin filaments
    • Vibert P., Craig R., Lehman W. Steric-model for activation of muscle thin filaments. J. Mol. Biol. 1997, 266:8-14.
    • (1997) J. Mol. Biol. , vol.266 , pp. 8-14
    • Vibert, P.1    Craig, R.2    Lehman, W.3
  • 34
    • 0018194371 scopus 로고
    • Study of tropomyosin labelled with a fluorescent probe by pulse fluorimetry in polarized light. Interaction of that protein with troponin and actin
    • Wahl P., Tawada K., Auchet J.C. Study of tropomyosin labelled with a fluorescent probe by pulse fluorimetry in polarized light. Interaction of that protein with troponin and actin. Eur. J. Biochem. 1978, 88:421-424.
    • (1978) Eur. J. Biochem. , vol.88 , pp. 421-424
    • Wahl, P.1    Tawada, K.2    Auchet, J.C.3
  • 35
    • 33845542919 scopus 로고    scopus 로고
    • Elasticity of α-helical coiled coils
    • Wolgemuth C.W., Sun S.X. Elasticity of α-helical coiled coils. Phys. Rev. Lett. 2006, 97:248101.
    • (2006) Phys. Rev. Lett. , vol.97 , pp. 248101
    • Wolgemuth, C.W.1    Sun, S.X.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.