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Volumn 83, Issue 5, 2002, Pages 2754-2766

Structure and interactions of the carboxyl terminus of striated muscle α-tropomyosin: It is important to be flexible

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA TROPOMYOSIN; TROPOMYOSIN; UNCLASSIFIED DRUG; PEPTIDE; RECOMBINANT PROTEIN;

EID: 0036842026     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(02)75285-5     Document Type: Article
Times cited : (49)

References (88)
  • 2
    • 0032897494 scopus 로고    scopus 로고
    • An analysis of conformational changes on protein-protein association: Implications for predictive docking
    • Betts, M. J., and M. J. Sternberg. 1999. An analysis of conformational changes on protein-protein association: Implications for predictive docking. Protein Eng. 12:271-283.
    • (1999) Protein Eng. , vol.12 , pp. 271-283
    • Betts, M.J.1    Sternberg, M.J.2
  • 3
    • 0000195671 scopus 로고
    • Natural abundance nitrogen-15 NMR by enhanced heteronuclear spectroscopy
    • Bodenhausen, G., and D. J. Ruben. 1980. Natural abundance nitrogen-15 NMR by enhanced heteronuclear spectroscopy. Chem. Phys. Lett. 69:185-189.
    • (1980) Chem. Phys. Lett. , vol.69 , pp. 185-189
    • Bodenhausen, G.1    Ruben, D.J.2
  • 4
    • 0026530383 scopus 로고
    • Quantitative analysis of protein far UV circular dichroism spectra by neural networks
    • Böhm, G., R. Muhr, and R. Jaenicke. 1992. Quantitative analysis of protein far UV circular dichroism spectra by neural networks. Protein Eng. 5:191-195.
    • (1992) Protein Eng. , vol.5 , pp. 191-195
    • Böhm, G.1    Muhr, R.2    Jaenicke, R.3
  • 5
    • 0348240665 scopus 로고
    • Four dimensional heteronuclear triple resonance NMR methods for the assignment of backbone nuclei in proteins
    • Boucher, W., E. D. Laue, S. L. Campbell-Burk, and P. J. Domaille. 1991. Four dimensional heteronuclear triple resonance NMR methods for the assignment of backbone nuclei in proteins. J. Am. Chem. Soc. 114:2262-2264.
    • (1991) J. Am. Chem. Soc. , vol.114 , pp. 2262-2264
    • Boucher, W.1    Laue, E.D.2    Campbell-Burk, S.L.3    Domaille, P.J.4
  • 7
    • 0036468396 scopus 로고    scopus 로고
    • Protein-protein association kinetics and protein docking
    • Camacho, C. J., and S. Vajda. 2002. Protein-protein association kinetics and protein docking. Curr. Opin. Struct. Biol. 12:36-40.
    • (2002) Curr. Opin. Struct. Biol. , vol.12 , pp. 36-40
    • Camacho, C.J.1    Vajda, S.2
  • 8
    • 0001170891 scopus 로고    scopus 로고
    • The carboxyl terminal amino acid residues glutamine276-threonine277 are important for actin affinity of the unacetylated smooth α-tropomyosin
    • Cho, Y. J. 2000. The carboxyl terminal amino acid residues glutamine276-threonine277 are important for actin affinity of the unacetylated smooth α-tropomyosin. J. Biochem. Mol. Biol. 33:531-536.
    • (2000) J. Biochem. Mol. Biol. , vol.33 , pp. 531-536
    • Cho, Y.J.1
  • 9
    • 0025787595 scopus 로고
    • Relationship between alternatively spliced exons and functional domains in tropomyosin
    • Cho, Y. J., and S. E. Hitchcock-DeGregori. 1991. Relationship between alternatively spliced exons and functional domains in tropomyosin. Proc. Natl. Acad. Sci. U. S. A. 88:10153-10157.
    • (1991) Proc. Natl. Acad. Sci. U. S. A. , vol.88 , pp. 10153-10157
    • Cho, Y.J.1    Hitchcock-DeGregori, S.E.2
  • 10
    • 0025105127 scopus 로고
    • The amino terminus of muscle tropomyosin is a major determinant for function
    • Cho, Y. J., J. Liu, and S. E. Hitchcock-DeGregori. 1990. The amino terminus of muscle tropomyosin is a major determinant for function. J. Biol. Chem. 265:538-545.
    • (1990) J. Biol. Chem. , vol.265 , pp. 538-545
    • Cho, Y.J.1    Liu, J.2    Hitchcock-DeGregori, S.E.3
  • 11
    • 0015967881 scopus 로고
    • Conformational parameters for amino acids in helical, beta-sheet, and random coil regions calculated from proteins
    • Chou, P. Y., and G. D. Fasman. 1974. Conformational parameters for amino acids in helical, beta-sheet, and random coil regions calculated from proteins. Biochemistry. 13:211-222.
    • (1974) Biochemistry , vol.13 , pp. 211-222
    • Chou, P.Y.1    Fasman, G.D.2
  • 13
    • 0020529404 scopus 로고
    • Some functional properties of nonpolymerizable and polymerizable tropomyosin
    • Dabrowska, R., E. Nowak, and W. Drabikowski. 1983. Some functional properties of nonpolymerizable and polymerizable tropomyosin. J. Muscle Res. Cell. Motil. 4:143-161.
    • (1983) J. Muscle Res. Cell. Motil. , vol.4 , pp. 143-161
    • Dabrowska, R.1    Nowak, E.2    Drabikowski, W.3
  • 14
    • 85031389992 scopus 로고    scopus 로고
    • Tropomyosin containing tryptophan analogs: Probes of specific thin filament protein interactions
    • de Sousa, A. D., and C. A. Farah. 2001. Tropomyosin containing tryptophan analogs: Probes of specific thin filament protein interactions. Biophys. J. 82:91a.
    • (2001) Biophys. J. , vol.82
    • De Sousa, A.D.1    Farah, C.A.2
  • 15
    • 0034663672 scopus 로고    scopus 로고
    • Interaction of the collagen-like tail of asymmetric acetylcholinesterase with heparin depends on triple-helical conformation, sequence and stability
    • Deprez, P., E. Doss-Pepe, B. Brodsky, and N. C. Inestrosa. 2000. Interaction of the collagen-like tail of asymmetric acetylcholinesterase with heparin depends on triple-helical conformation, sequence and stability. Biochem. J. 350:283-290.
    • (2000) Biochem. J. , vol.350 , pp. 283-290
    • Deprez, P.1    Doss-Pepe, E.2    Brodsky, B.3    Inestrosa, N.C.4
  • 16
    • 0034610302 scopus 로고    scopus 로고
    • Interaction of collagen-like peptide models of asymmetric acetylcholinesterase with glycosaminoglycans: Spectroscopic studies of conformational changes and stability
    • Doss-Pepe, E., P. Deprez, N. C. Inestrosa, and B. Brodsky. 2000. Interaction of collagen-like peptide models of asymmetric acetylcholinesterase with glycosaminoglycans: Spectroscopic studies of conformational changes and stability. Biochemistry. 39:14884-14892.
    • (2000) Biochemistry , vol.39 , pp. 14884-14892
    • Doss-Pepe, E.1    Deprez, P.2    Inestrosa, N.C.3    Brodsky, B.4
  • 17
    • 0030184317 scopus 로고    scopus 로고
    • Phase labeling of C-H and C-C spin-system topologies: Application in PFG-HACANH and PFG-HACA(CO)NH triple-resonance experiments for determining backbone resonance assignments in proteins
    • Feng, W., C. B. Rios, and G. T. Montelione. 1996. Phase labeling of C-H and C-C spin-system topologies: Application in PFG-HACANH and PFG-HACA(CO)NH triple-resonance experiments for determining backbone resonance assignments in proteins. J. Biomol. Nucl. Magn. Reson. 8:98-104.
    • (1996) J. Biomol. Nucl. Magn. Reson. , vol.8 , pp. 98-104
    • Feng, W.1    Rios, C.B.2    Montelione, G.T.3
  • 18
    • 0026253633 scopus 로고
    • The helix-coil transition in heterogeneous peptides with specific side-chain interactions: Theory and comparison with CD spectral data
    • Gans, P. J., P. C. Lyu, M. C. Manning, R. W. Woody, and N. R. Kallenbach. 1991. The helix-coil transition in heterogeneous peptides with specific side-chain interactions: Theory and comparison with CD spectral data. Biopolymers. 31:1605-1614.
    • (1991) Biopolymers , vol.31 , pp. 1605-1614
    • Gans, P.J.1    Lyu, P.C.2    Manning, M.C.3    Woody, R.W.4    Kallenbach, N.R.5
  • 19
    • 0017344431 scopus 로고
    • Molecular aspects of muscle contraction and regulation
    • Gergely, J. 1977. Molecular aspects of muscle contraction and regulation. Basic Res. Cardiol. 72:109-117.
    • (1977) Basic Res. Cardiol. , vol.72 , pp. 109-117
    • Gergely, J.1
  • 20
    • 0026317334 scopus 로고
    • Periodicity of amide proton exchange rates in a coiled-coil leucine zipper peptide
    • Goodman, E. M., and P. S. Kim, 1991. Periodicity of amide proton exchange rates in a coiled-coil leucine zipper peptide. Biochemistry. 30:11615-11620.
    • (1991) Biochemistry , vol.30 , pp. 11615-11620
    • Goodman, E.M.1    Kim, P.S.2
  • 21
    • 0034059761 scopus 로고    scopus 로고
    • Regulation of contraction in striated muscle
    • Gordon, A. M., E. Homsher, and M. Regnier. 2000. Regulation of contraction in striated muscle. Physiol. Rev. 80:853-924.
    • (2000) Physiol. Rev. , vol.80 , pp. 853-924
    • Gordon, A.M.1    Homsher, E.2    Regnier, M.3
  • 22
    • 0036232091 scopus 로고    scopus 로고
    • Tropomyosin requires an intact N-terminal coiled coil to interact with tropomodulin
    • Greenfield, N. J., and V. M. Fowler. 2002. Tropomyosin requires an intact N-terminal coiled coil to interact with tropomodulin. Biophys. J. 82:2580-2591.
    • (2002) Biophys. J. , vol.82 , pp. 2580-2591
    • Greenfield, N.J.1    Fowler, V.M.2
  • 23
    • 0035965135 scopus 로고    scopus 로고
    • Solution NMR structure and folding dynamics of the N terminus of a rat non-muscle a-tropomyosin in an engineered chimeric protein
    • Greenfield, N. J., J. H. Huang, T. Palm, G. V. T. Swapna, D. Monleon, G. T. Montelione, and S. E. Hitchcock-DeGregori. 2001. Solution NMR structure and folding dynamics of the N terminus of a rat non-muscle a-tropomyosin in an engineered chimeric protein. J. Mol. Biol. 312:833-847.
    • (2001) J. Mol. Biol. , vol.312 , pp. 833-847
    • Greenfield, N.J.1    Huang, J.H.2    Palm, T.3    Swapna, G.V.T.4    Monleon, D.5    Montelione, G.T.6    Hitchcock-DeGregori, S.E.7
  • 24
    • 0032568543 scopus 로고    scopus 로고
    • The structure of the N-terminus of striated muscle alpha-tropomyosin in a chimeric peptide: Nuclear magnetic resonance structure and circular dichroism studies
    • Greenfield, N. J., G. T. Montelione, R. S. Farid, and S. E. Hitchcock-DeGregori, 1998. The structure of the N-terminus of striated muscle alpha-tropomyosin in a chimeric peptide: Nuclear magnetic resonance structure and circular dichroism studies. Biochemistry. 37:7834-7843.
    • (1998) Biochemistry , vol.37 , pp. 7834-7843
    • Greenfield, N.J.1    Montelione, G.T.2    Farid, R.S.3    Hitchcock-DeGregori, S.E.4
  • 25
    • 0028258048 scopus 로고
    • The effect of N-terminal acetylation on the structure of an N-terminal tropomyosin peptide and alpha alpha-tropomyosin
    • Greenfield, N. J., W. F. Stafford, and S. E. Hitchcock-DeGregori. 1994. The effect of N-terminal acetylation on the structure of an N-terminal tropomyosin peptide and alpha alpha-tropomyosin. Protein Sci. 3:402-410.
    • (1994) Protein Sci. , vol.3 , pp. 402-410
    • Greenfield, N.J.1    Stafford, W.F.2    Hitchcock-DeGregori, S.E.3
  • 26
    • 9444245493 scopus 로고
    • Correlating backbone amide and sidechain resonances in larger proteins by multiple relay triple resonance NMR
    • Grzesiek, S., and A, Bax. 1992a. Correlating backbone amide and sidechain resonances in larger proteins by multiple relay triple resonance NMR. J. Am. Chem. Soc. 114:6291-6293.
    • (1992) J. Am. Chem. Soc. , vol.114 , pp. 6291-6293
    • Grzesiek, S.1    Bax, A.2
  • 27
    • 44049109615 scopus 로고
    • An efficient experiment for sequential backbone assignment of medium-sized isotopically enriched proteins
    • Grzesiek, S., and A. Bax. 1992b. An efficient experiment for sequential backbone assignment of medium-sized isotopically enriched proteins. J. Magn. Reson. 99:201-207.
    • (1992) J. Magn. Reson. , vol.99 , pp. 201-207
    • Grzesiek, S.1    Bax, A.2
  • 28
    • 0030067632 scopus 로고    scopus 로고
    • Mapping the functional domains within the carboxyl terminus of alpha-tropomyosin encoded by the alternatively spliced ninth exon
    • Hammell, R. L., and S. E. Hitchcock-DeGregori. 1996. Mapping the functional domains within the carboxyl terminus of alpha-tropomyosin encoded by the alternatively spliced ninth exon. J. Biol. Chem. 271:4236-4242.
    • (1996) J. Biol. Chem. , vol.271 , pp. 4236-4242
    • Hammell, R.L.1    Hitchcock-DeGregori, S.E.2
  • 29
    • 0030884448 scopus 로고    scopus 로고
    • The sequence of the alternatively spliced sixth exon of alpha-tropomyosin is critical for cooperative actin binding but not for interaction with troponin
    • Hammell, R. L., and S. E. Hitchcock-DeGregori. 1997. The sequence of the alternatively spliced sixth exon of alpha-tropomyosin is critical for cooperative actin binding but not for interaction with troponin. J. Biol. Chem. 272:22409-22416.
    • (1997) J. Biol. Chem. , vol.272 , pp. 22409-22416
    • Hammell, R.L.1    Hitchcock-DeGregori, S.E.2
  • 30
    • 0024513868 scopus 로고
    • Effects of deletion of tropomyosin overlap on regulated actomyosin subfragment 1 ATPase
    • Heeley, D. H., L. B. Smillie, and E. M. Lohmeier-Vogel. 1989. Effects of deletion of tropomyosin overlap on regulated actomyosin subfragment 1 ATPase. Biochem. J. 258:831-836.
    • (1989) Biochem. J. , vol.258 , pp. 831-836
    • Heeley, D.H.1    Smillie, L.B.2    Lohmeier-Vogel, E.M.3
  • 31
    • 0011091549 scopus 로고    scopus 로고
    • Tropomyosin
    • T. Creighton, editor. John Wiley and Sons, New York
    • Hitchcock-DeGregori, S. E. 2002. Tropomyosin. In Encyclopeida of Molecular Medicine. T. Creighton, editor. John Wiley and Sons, New York. 3247-3251.
    • (2002) Encyclopeida of Molecular Medicine , pp. 3247-3251
    • Hitchcock-DeGregori, S.E.1
  • 32
    • 0019493825 scopus 로고
    • Synthetic model for two-stranded alpha-helical coiled-coils. Design, synthesis, and characterization of an 86-residue analog of tropomyosin
    • Hodges, R. S., A. K. Saund, P. C. Chong, S. A. St.-Pierre, and R. E.- Reid. 1981. Synthetic model for two-stranded alpha-helical coiled-coils. Design, synthesis, and characterization of an 86-residue analog of tropomyosin. J. Biol. Chem. 256:1214-1224.
    • (1981) J. Biol. Chem. , vol.256 , pp. 1214-1224
    • Hodges, R.S.1    Saund, A.K.2    Chong, P.C.3    St.-Pierre, S.A.4    Reid, R.E.5
  • 33
    • 0028816067 scopus 로고
    • Structural stability of short subsequences of the tropomyosin chain
    • Holtzer, M. E., D. L. Crimmins, and A. Holtzer. 1995. Structural stability of short subsequences of the tropomyosin chain. Biopolymers. 35:125-136.
    • (1995) Biopolymers , vol.35 , pp. 125-136
    • Holtzer, M.E.1    Crimmins, D.L.2    Holtzer, A.3
  • 34
    • 0025681523 scopus 로고
    • Alpha-helix to random coil transitions of two-chain coiled coils: Experiments on the thermal denaturation of isolated segments of alpha alpha-tropomyosin
    • Holtzer, M. E., and A. Holtzer. 1990. Alpha-helix to random coil transitions of two-chain coiled coils: Experiments on the thermal denaturation of isolated segments of alpha alpha-tropomyosin. Biopolymers. 30:985-993.
    • (1990) Biopolymers , vol.30 , pp. 985-993
    • Holtzer, M.E.1    Holtzer, A.2
  • 35
    • 0027074092 scopus 로고
    • Unfolding domains of recombinant fusion alpha alpha-tropomyosin
    • Ishii, Y., S. Hitchcock-DeGregori, K. Mabuchi, and S. S. Lehrer. 1992. Unfolding domains of recombinant fusion alpha alpha-tropomyosin. Protein Sci. 1:1319-1325.
    • (1992) Protein Sci. , vol.1 , pp. 1319-1325
    • Ishii, Y.1    Hitchcock-DeGregori, S.2    Mabuchi, K.3    Lehrer, S.S.4
  • 36
    • 15844402153 scopus 로고    scopus 로고
    • High resolution NMR solution structure of the leucine zipper domain of the c-Jun homodimer
    • Junius, F. K., S. I. O'Donoghue, M. Nilges, A. S. Weiss, and G. F. King. 1996. High resolution NMR solution structure of the leucine zipper domain of the c-Jun homodimer. J. Biol. Chem. 271:13663-13667.
    • (1996) J. Biol. Chem. , vol.271 , pp. 13663-13667
    • Junius, F.K.1    O'Donoghue, S.I.2    Nilges, M.3    Weiss, A.S.4    King, G.F.5
  • 37
    • 0028676245 scopus 로고
    • Protein-protein interaction: Complex flexibility
    • Jurnak, F. 1994. Protein-protein interaction: Complex flexibility. Nature. 372:409-410.
    • (1994) Nature , vol.372 , pp. 409-410
    • Jurnak, F.1
  • 38
    • 0020119146 scopus 로고
    • Ca2+-dependent binding of synthetic peptides corresponding to some regions of troponin-I to troponin-C
    • Katayama, E., and S. Nozaki. 1982. Ca2+-dependent binding of synthetic peptides corresponding to some regions of troponin-I to troponin-C. J. Biochem. (Tokyo). 91:1449-1452.
    • (1982) J. Biochem. (Tokyo) , vol.91 , pp. 1449-1452
    • Katayama, E.1    Nozaki, S.2
  • 39
    • 0025374145 scopus 로고
    • Proton proton correlation via carbon-carbon couplings: A three dimensional NMR approach for the assignment of aliphatic resonances in proteins labeled with C-13
    • Kay, L. E., M. Ikura, and A. Bax. 1990. Proton proton correlation via carbon-carbon couplings: A three dimensional NMR approach for the assignment of aliphatic resonances in proteins labeled with C-13. J. Am. Chem. Soc. 112:888-889.
    • (1990) J. Am. Chem. Soc. , vol.112 , pp. 888-889
    • Kay, L.E.1    Ikura, M.2    Bax, A.3
  • 40
    • 0006925492 scopus 로고
    • Pure absorption gradient enhanced heteronuclear single quantum correlation spectroscopy with improved sensitivity
    • Kay, L. E., P. Keifer, and T. Saarinen. 1992. Pure absorption gradient enhanced heteronuclear single quantum correlation spectroscopy with improved sensitivity. J. Am. Chem. Soc. 114:10663-10665.
    • (1992) J. Am. Chem. Soc. , vol.114 , pp. 10663-10665
    • Kay, L.E.1    Keifer, P.2    Saarinen, T.3
  • 41
    • 0017893055 scopus 로고
    • Effects of an interchain disulfide bond on tropomyosin structure: Differential scanning calorimetry
    • Krishnan, K. S., J. F. Brandts, and S. S. Lehrer. 1978. Effects of an interchain disulfide bond on tropomyosin structure: Differential scanning calorimetry. FEBS Lett. 91:206-208.
    • (1978) FEBS Lett. , vol.91 , pp. 206-208
    • Krishnan, K.S.1    Brandts, J.F.2    Lehrer, S.S.3
  • 42
    • 0024295767 scopus 로고
    • The leucine zipper: A hypothetical structure common to a new class of DNA binding proteins
    • Landschulz, W. H., P. F. Johnson, and S. L. McKnight. 1988. The leucine zipper: A hypothetical structure common to a new class of DNA binding proteins. Science. 240:1759-1764.
    • (1988) Science , vol.240 , pp. 1759-1764
    • Landschulz, W.H.1    Johnson, P.F.2    McKnight, S.L.3
  • 43
    • 0016774006 scopus 로고
    • Intramolecular crosslinking of tropomyosin via disulfide bond formation: Evidence for chain register
    • Lehrer, S. S. 1975. Intramolecular crosslinking of tropomyosin via disulfide bond formation: Evidence for chain register. Proc. Natl. Acad. Sci. U. S. A. 72:3377-3381.
    • (1975) Proc. Natl. Acad. Sci. U. S. A. , vol.72 , pp. 3377-3381
    • Lehrer, S.S.1
  • 44
    • 0017849306 scopus 로고
    • Effects of an interchain disulfide bond on tropomyosin structure: Intrinsic fluorescence and circular dichroism studies
    • Lehrer, S. S. 1978. Effects of an interchain disulfide bond on tropomyosin structure: Intrinsic fluorescence and circular dichroism studies. J. Mol. Biol. 118:209-226.
    • (1978) J. Mol. Biol. , vol.118 , pp. 209-226
    • Lehrer, S.S.1
  • 45
    • 0032540229 scopus 로고    scopus 로고
    • The muscle thin filament as a classical cooperative/allosteric regulatory system
    • Lehrer, S. S., and M. A. Geeves. 1998. The muscle thin filament as a classical cooperative/allosteric regulatory system. J. Mol. Biol. 277:1081-1089.
    • (1998) J. Mol. Biol. , vol.277 , pp. 1081-1089
    • Lehrer, S.S.1    Geeves, M.A.2
  • 46
    • 0030838333 scopus 로고    scopus 로고
    • Actin-tropomyosin activation of myosin subfragment 1 ATPase and thin filament cooperativity: The role of tropomyosin flexibility and end-to-end interactions
    • Lehrer, S. S., N. L. Golitsina, and M. A. Geeves. 1997. Actin-tropomyosin activation of myosin subfragment 1 ATPase and thin filament cooperativity: The role of tropomyosin flexibility and end-to-end interactions. Biochemistry. 36:13449-13454.
    • (1997) Biochemistry , vol.36 , pp. 13449-13454
    • Lehrer, S.S.1    Golitsina, N.L.2    Geeves, M.A.3
  • 47
    • 0037188485 scopus 로고    scopus 로고
    • The crystal structure of the C-terminal fragment of striated-muscle alpha-tropomyosin reveals a key troponin T recognition site
    • Li, Y., S. Mui, J. H. Brown, J. Strand, L. Reshetnikova, L. S. Tobacman, and C. Cohen. 2002. The crystal structure of the C-terminal fragment of striated-muscle alpha-tropomyosin reveals a key troponin T recognition site. Proc. Natl. Acad. Sci. U.S.A. 99:7378-7383.
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 7378-7383
    • Li, Y.1    Mui, S.2    Brown, J.H.3    Strand, J.4    Reshetnikova, L.5    Tobacman, L.S.6    Cohen, C.7
  • 48
    • 0019882706 scopus 로고
    • Non-polymerizable tropomyosin: Preparation, some properties and F-actin binding
    • Mak, A. S., and L. B. Smillie. 1981. Non-polymerizable tropomyosin: Preparation, some properties and F-actin binding. Biochem. Biophys. Res. Commun. 101:208-214.
    • (1981) Biochem. Biophys. Res. Commun. , vol.101 , pp. 208-214
    • Mak, A.S.1    Smillie, L.B.2
  • 49
    • 0034711008 scopus 로고    scopus 로고
    • Interhelical ion pairing in coiled coils: Solution structure of a heterodimeric leucine zipper and determination of pK(a) values of glu side chains
    • Marti, D. N., I. Jelesarov, and H. R. Bosshard. 2000. Interhelical ion pairing in coiled coils: Solution structure of a heterodimeric leucine zipper and determination of pK(a) values of glu side chains. Biochemistry. 39:12804-12818.
    • (2000) Biochemistry , vol.39 , pp. 12804-12818
    • Marti, D.N.1    Jelesarov, I.2    Bosshard, H.R.3
  • 50
    • 0016774265 scopus 로고
    • Tropomyosin coiled-coil interactions: Evidence for an unstaggered structure
    • McLachlan, A. D., and M. Stewart. 1975. Tropomyosin coiled-coil interactions: Evidence for an unstaggered structure. J. Mol. Biol. 98:293-304.
    • (1975) J. Mol. Biol. , vol.98 , pp. 293-304
    • McLachlan, A.D.1    Stewart, M.2
  • 51
    • 0000433362 scopus 로고
    • HN-H coupling constants in polypeptides using heteronuclear 2-D NMR experiments
    • HN-H coupling constants in polypeptides using heteronuclear 2-D NMR experiments. J. Am. Chem. Soc. 111:5474-5475.
    • (1989) J. Am. Chem. Soc. , vol.111 , pp. 5474-5475
    • Montelione, G.T.1    Wagner, G.2
  • 53
    • 0011110068 scopus 로고    scopus 로고
    • S1-induced actin binding of tropomyosin depends on its C terminus
    • Moraczewska, J., and S. E. Hitchcock-DeGregori. 1998. S1-induced actin binding of tropomyosin depends on its C terminus. Biophys. J. 74:532.
    • (1998) Biophys. J. , vol.74 , pp. 532
    • Moraczewska, J.1    Hitchcock-DeGregori, S.E.2
  • 54
    • 0034643863 scopus 로고    scopus 로고
    • Independent functions for the N- and C-termini in the overlap region of tropomyosin
    • Moraczewska, J., and S. E. Hitchcock-DeGregori. 2000. Independent functions for the N- and C-termini in the overlap region of tropomyosin. Biochemistry. 39:6891-6897.
    • (2000) Biochemistry , vol.39 , pp. 6891-6897
    • Moraczewska, J.1    Hitchcock-DeGregori, S.E.2
  • 55
    • 0033619726 scopus 로고    scopus 로고
    • The ends of tropomyosin are major determinants of actin affinity and myosin subfragment 1-induced binding to F-actin in the open state
    • Moraczewska, J., K. Nicholson-Flynn, and S. E. Hitchcock-DeGregori. 1999. The ends of tropomyosin are major determinants of actin affinity and myosin subfragment 1-induced binding to F-actin in the open state. Biochemistry. 38:15885-15892.
    • (1999) Biochemistry , vol.38 , pp. 15885-15892
    • Moraczewska, J.1    Nicholson-Flynn, K.2    Hitchcock-DeGregori, S.E.3
  • 56
    • 0001689741 scopus 로고
    • Gradient-enhanced tripleresonance three-dimensional NMR experiments with improved sensitivity
    • Muhandiram, D. R., and L. E. Kay. 1994. Gradient-enhanced tripleresonance three-dimensional NMR experiments with improved sensitivity. J. Magn. Reson. Ser. B. 103:203-216.
    • (1994) J. Magn. Reson. Ser. B , vol.103 , pp. 203-216
    • Muhandiram, D.R.1    Kay, L.E.2
  • 57
    • 0025272236 scopus 로고
    • Secondary structure of a leucine zipper determined by nuclear magnetic resonance spectroscopy
    • Oas, T. G., L. P. McIntosh, E. K. O'Shea, F. W. Dahlquist, and P. S. Kim. 1990. Secondary structure of a leucine zipper determined by nuclear magnetic resonance spectroscopy. Biochemistry. 29:2891-2894.
    • (1990) Biochemistry , vol.29 , pp. 2891-2894
    • Oas, T.G.1    McIntosh, L.P.2    O'Shea, E.K.3    Dahlquist, F.W.4    Kim, P.S.5
  • 58
    • 0016871495 scopus 로고
    • Studies on calcium ion-induced conformation changes in the actin-tropomyosin-troponin system by fluorimetry: III. Changes in the conformation of tropomyosin associated with functional states
    • Ohyashiki, T., Y. Kanaoka, and T. Sekine. 1976. Studies on calcium ion-induced conformation changes in the actin-tropomyosin-troponin system by fluorimetry: III. Changes in the conformation of tropomyosin associated with functional states. Biochim. Biophys. Acta. 420:27-36.
    • (1976) Biochim. Biophys. Acta , vol.420 , pp. 27-36
    • Ohyashiki, T.1    Kanaoka, Y.2    Sekine, T.3
  • 59
    • 0034623135 scopus 로고    scopus 로고
    • Mapping the domain of troponin T responsible for the activation of actomyosin ATPase activity: Identification of residues involved in binding to actin
    • Oliveira, D. M., C. R. Nakaie, A. D. Sousa, C. S. Farah, and F. C. Reinach. 2000. Mapping the domain of troponin T responsible for the activation of actomyosin ATPase activity: Identification of residues involved in binding to actin. J. Biol. Chem. 275:27513-27519.
    • (2000) J. Biol. Chem. , vol.275 , pp. 27513-27519
    • Oliveira, D.M.1    Nakaie, C.R.2    Sousa, A.D.3    Farah, C.S.4    Reinach, F.C.5
  • 60
    • 0025222978 scopus 로고
    • A thermodynamic scale for the helix-forming tendencies of the commonly occurring amino acids
    • O'Neil, K. T., and W. F. DeGrado. 1990. A thermodynamic scale for the helix-forming tendencies of the commonly occurring amino acids. Science. 250:646-651.
    • (1990) Science , vol.250 , pp. 646-651
    • O'Neil, K.T.1    DeGrado, W.F.2
  • 61
    • 0034759429 scopus 로고    scopus 로고
    • Disease-causing mutations in cardiac troponin T: Identification of a critical tropomyosin-binding region
    • Palm, T., S. Graboski, S. E. Hitchcock-DeGregori, and N. J. Greenfield. 2001. Disease-causing mutations in cardiac troponin T: Identification of a critical tropomyosin-binding region. Biophys. J. 81:2827-2837.
    • (2001) Biophys. J. , vol.81 , pp. 2827-2837
    • Palm, T.1    Graboski, S.2    Hitchcock-DeGregori, S.E.3    Greenfield, N.J.4
  • 62
    • 0024349096 scopus 로고
    • Removal of tropomyosin overlap modifies cooperative binding of myosin S-1 to reconstituted thin filaments of rabbit striated muscle
    • Pan, B. S., A. M. Gordon, and Z. X. Luo. 1989. Removal of tropomyosin overlap modifies cooperative binding of myosin S-1 to reconstituted thin filaments of rabbit striated muscle. J. Biol. Chem. 264:8495-8498.
    • (1989) J. Biol. Chem. , vol.264 , pp. 8495-8498
    • Pan, B.S.1    Gordon, A.M.2    Luo, Z.X.3
  • 63
    • 0034841005 scopus 로고    scopus 로고
    • Vertebrate tropomyosin: Distribution, properties and function
    • Perry, S. V. 2001. Vertebrate tropomyosin: Distribution, properties and function. J. Muscle Res. Cell Motil. 22:5-49.
    • (2001) J. Muscle Res. Cell Motil. , vol.22 , pp. 5-49
    • Perry, S.V.1
  • 64
    • 0023042854 scopus 로고
    • Construction of an atomic model for tropomyosin and implications for interactions with actin
    • Phillips, G. N., Jr. 1986. Construction of an atomic model for tropomyosin and implications for interactions with actin. J. Mol. Biol. 192:128-131.
    • (1986) J. Mol. Biol. , vol.192 , pp. 128-131
    • Phillips G.N., Jr.1
  • 65
    • 0030021059 scopus 로고    scopus 로고
    • Mechanical properties of tropomyosin and implications for muscle regulation
    • Phillips, G. N., Jr., and S. Chacko. 1996. Mechanical properties of tropomyosin and implications for muscle regulation. Biopolymers. 38:89-95.
    • (1996) Biopolymers , vol.38 , pp. 89-95
    • Phillips G.N., Jr.1    Chacko, S.2
  • 66
    • 0019075125 scopus 로고
    • Motions of tropomyosin: Crystal as metaphor
    • Phillips, G. N., Jr., J. P. Fillers, and C. Cohen. 1980. Motions of tropomyosin: Crystal as metaphor. Biophys. J. 32:485-502.
    • (1980) Biophys. J. , vol.32 , pp. 485-502
    • Phillips G.N., Jr.1    Fillers, J.P.2    Cohen, C.3
  • 67
    • 0023042847 scopus 로고
    • Tropomyosin crystal structure and muscle regulation
    • Phillips, G. N., Jr., J. P. Fillers, and C. Cohen. 1986. Tropomyosin crystal structure and muscle regulation. J. Mol. Biol. 192:111-131.
    • (1986) J. Mol. Biol. , vol.192 , pp. 111-131
    • Phillips G.N., Jr.1    Fillers, J.P.2    Cohen, C.3
  • 68
    • 0018803780 scopus 로고
    • Crystal structure and molecular interactions of tropomyosin
    • Phillips, G. N., Jr., E. E. Lattman, P. Cummins, K. Y. Lee, and C. Cohen. 1979. Crystal structure and molecular interactions of tropomyosin. Nature. 278:413-417.
    • (1979) Nature , vol.278 , pp. 413-417
    • Phillips G.N., Jr.1    Lattman, E.E.2    Cummins, P.3    Lee, K.Y.4    Cohen, C.5
  • 69
    • 0020483742 scopus 로고
    • Co-operative blocks in tropomyosin
    • Potekhin, S. A., and P. L. Privalov. 1982. Co-operative blocks in tropomyosin. J. Mol. Biol. 159:519-535.
    • (1982) J. Mol. Biol. , vol.159 , pp. 519-535
    • Potekhin, S.A.1    Privalov, P.L.2
  • 70
    • 0020348367 scopus 로고
    • Stability of proteins: Proteins which do not present a single cooperative system
    • Privalov, P. L. 1982. Stability of proteins: Proteins which do not present a single cooperative system. Adv. Protein Chem. 35:1-104.
    • (1982) Adv. Protein Chem. , vol.35 , pp. 1-104
    • Privalov, P.L.1
  • 71
    • 0030256487 scopus 로고    scopus 로고
    • Phase labeling of C-H and C-C spin-system topologies: Application in constant-time PFG-CBCA(CO)NH experiments for discriminating amino acid spin-system types
    • Rios, C. B., W. Feng, M. Tashiro, Z. Shang, and G. T. Montelione. 1996. Phase labeling of C-H and C-C spin-system topologies: Application in constant-time PFG-CBCA(CO)NH experiments for discriminating amino acid spin-system types. J. Biomol. Nucl. Magn. Reson. 8:345-350.
    • (1996) J. Biomol. Nucl. Magn. Reson. , vol.8 , pp. 345-350
    • Rios, C.B.1    Feng, W.2    Tashiro, M.3    Shang, Z.4    Montelione, G.T.5
  • 72
    • 0023180728 scopus 로고
    • Alpha-tropomyosin gene organization: Alternative splicing of duplicated isotype-specific exons accounts for the production of smooth and striated muscle isoforms
    • Ruiz-Opazo, N., and B. Nadal-Ginard. 1987. Alpha-tropomyosin gene organization: Alternative splicing of duplicated isotype-specific exons accounts for the production of smooth and striated muscle isoforms. J. Biol. Chem. 262:4755-4765.
    • (1987) J. Biol. Chem. , vol.262 , pp. 4755-4765
    • Ruiz-Opazo, N.1    Nadal-Ginard, B.2
  • 73
    • 0033917257 scopus 로고    scopus 로고
    • The effect of single residue substitution of serine-283 on the strength of head-to-tail interaction and actin binding properties of rabbit skeletal muscle alphatropomyosin
    • Sano, K., K. Maeda, T. Oda, and Y. Maeda. 2000. The effect of single residue substitution of serine-283 on the strength of head-to-tail interaction and actin binding properties of rabbit skeletal muscle alphatropomyosin. J. Biochem. (Tokyo). 237:1095-1102.
    • (2000) J. Biochem. (Tokyo) , vol.237 , pp. 1095-1102
    • Sano, K.1    Maeda, K.2    Oda, T.3    Maeda, Y.4
  • 74
    • 0028831760 scopus 로고
    • Improved high-level expression system for eukaryotic genes in Escherichia coli using T7 RNA polymerase and rare ArgtRNAs
    • Schenk, P. M., S. Baumann, R. Mattes, and H. H. Steinbiss. 1995. Improved high-level expression system for eukaryotic genes in Escherichia coli using T7 RNA polymerase and rare ArgtRNAs. Biotechniques. 19:196-198.
    • (1995) Biotechniques , vol.19 , pp. 196-198
    • Schenk, P.M.1    Baumann, S.2    Mattes, R.3    Steinbiss, H.H.4
  • 75
    • 0033794319 scopus 로고    scopus 로고
    • Random coil chemical shifts in acidic 8 M urea: Implementation of random coil shift data in NMRView
    • Schwarzinger, S., G. J. Kroon, T. R. Foss, P. E. Wright, and H. J. Dyson. 2000. Random coil chemical shifts in acidic 8 M urea: Implementation of random coil shift data in NMRView. J. Biomol. Nucl. Magn. Reson. 18:43-48.
    • (2000) J. Biomol. Nucl. Magn. Reson. , vol.18 , pp. 43-48
    • Schwarzinger, S.1    Kroon, G.J.2    Foss, T.R.3    Wright, P.E.4    Dyson, H.J.5
  • 76
    • 0021103964 scopus 로고
    • Nuclear magnetic resonance evidence for a flexible region at the C terminus of alpha-tropomyosin
    • Stewart, M., and G. C. Roberts. 1983. Nuclear magnetic resonance evidence for a flexible region at the C terminus of alpha-tropomyosin. J. Mol. Biol. 166:219-225.
    • (1983) J. Mol. Biol. , vol.166 , pp. 219-225
    • Stewart, M.1    Roberts, G.C.2
  • 78
    • 0026143165 scopus 로고
    • A scanning calorimetric study of the thermally induced unfolding of various forms of tropomyosin
    • Sturtevant, J. M., M. E. Holtzer, and A. Holtzer. 1991. A scanning calorimetric study of the thermally induced unfolding of various forms of tropomyosin. Biopolymers. 31:489-495.
    • (1991) Biopolymers , vol.31 , pp. 489-495
    • Sturtevant, J.M.1    Holtzer, M.E.2    Holtzer, A.3
  • 79
    • 0034660904 scopus 로고    scopus 로고
    • Luxury accommodations: The expanding role of structural plasticity in protein-protein interactions
    • Sundberg, E. J., and R. A. Mariuzza. 2000. Luxury accommodations: The expanding role of structural plasticity in protein-protein interactions. Struct. Fold Des. 8:R137-142.
    • (2000) Struct. Fold Des. , vol.8
    • Sundberg, E.J.1    Mariuzza, R.A.2
  • 80
    • 0016768185 scopus 로고
    • Non-polymerizable tropomyosin and control of the superprecipitation of actomyosin
    • Tawada, Y., H. Oara, T. Ooi, and K. Tawada. 1975. Non-polymerizable tropomyosin and control of the superprecipitation of actomyosin. Biochemistry. 78:65-72.
    • (1975) Biochemistry , vol.78 , pp. 65-72
    • Tawada, Y.1    Oara, H.2    Ooi, T.3    Tawada, K.4
  • 81
    • 0034616959 scopus 로고    scopus 로고
    • Effects of side-chain characteristics on stability and oligomerization state of a de novo-designed model coiled-coil: 20 Amino acid substitutions in position "d."
    • Tripet, B., K. Wagschal, P. Lavigne, C. T. Mant, and R. S. Hodges. 2000. Effects of side-chain characteristics on stability and oligomerization state of a de novo-designed model coiled-coil: 20 Amino acid substitutions in position "d." J. Mol, Biol. 300:377-402.
    • (2000) J. Mol. Biol. , vol.300 , pp. 377-402
    • Tripet, B.1    Wagschal, K.2    Lavigne, P.3    Mant, C.T.4    Hodges, R.S.5
  • 82
    • 0032720311 scopus 로고    scopus 로고
    • The role of position a in determining the stability and oligomerization state of alpha-helical coiled coils: 20 Amino acid stability coefficients in the hydrophobic core of proteins
    • Wagschal, K., B. Tripet, P. Lavigne, C. Mant, and R. S. Hodges. 1999. The role of position a in determining the stability and oligomerization state of alpha-helical coiled coils: 20 Amino acid stability coefficients in the hydrophobic core of proteins. Protein Sci. 8:2312-2329.
    • (1999) Protein Sci. , vol.8 , pp. 2312-2329
    • Wagschal, K.1    Tripet, B.2    Lavigne, P.3    Mant, C.4    Hodges, R.S.5
  • 83
    • 0022429269 scopus 로고
    • Removal of tropomyosin overlap and the co-operative response to increasing calcium concentrations of the acto-subfragment-1 ATPase
    • Walsh, T. P., C. E. Trueblood, R. Evans, and A. Weber. 1985. Removal of tropomyosin overlap and the co-operative response to increasing calcium concentrations of the acto-subfragment-1 ATPase. J. Mol. Biol. 182:265-269.
    • (1985) J. Mol. Biol. , vol.182 , pp. 265-269
    • Walsh, T.P.1    Trueblood, C.E.2    Evans, R.3    Weber, A.4
  • 84
    • 0033985268 scopus 로고    scopus 로고
    • Crystal structure of tropomyosin at 7 Angstroms resolution
    • Whitby, F. G., and G. N. Phillips, Jr. 2000. Crystal structure of tropomyosin at 7 Angstroms resolution. Proteins. 38:49-59.
    • (2000) Proteins , vol.38 , pp. 49-59
    • Whitby, F.G.1    Phillips G.N., Jr.2
  • 86
    • 0026597879 scopus 로고
    • The chemical shift index: A fast and simple method for the assignment of protein secondary structure through NMR spectroscopy
    • Wishart, D. S., B. D. Sykes, and F. M. Richards. 1992. The chemical shift index: A fast and simple method for the assignment of protein secondary structure through NMR spectroscopy. Biochemistry. 31:1647-1651.
    • (1992) Biochemistry , vol.31 , pp. 1647-1651
    • Wishart, D.S.1    Sykes, B.D.2    Richards, F.M.3
  • 87
    • 0027480940 scopus 로고
    • Disulfide bond contribution to protein stability: Positional effects of substitution in the hydrophobic core of the two-stranded alpha-helical coiled-coil
    • Zhou, N. E., C. M. Kay, and R. S. Hodges. 1993. Disulfide bond contribution to protein stability: Positional effects of substitution in the hydrophobic core of the two-stranded alpha-helical coiled-coil. Biochemistry. 32:3178-3187.
    • (1993) Biochemistry , vol.32 , pp. 3178-3187
    • Zhou, N.E.1    Kay, C.M.2    Hodges, R.S.3


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