메뉴 건너뛰기




Volumn 257, Issue 2, 1996, Pages 367-384

Correlation between conformational and binding properties of nebulin repeats

Author keywords

Actin; Muscle; Structure; Thin filament

Indexed keywords

F ACTIN; NEBULIN; SYNTHETIC PEPTIDE; TRIFLUOROETHANOL;

EID: 0029966287     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1996.0169     Document Type: Article
Times cited : (63)

References (46)
  • 1
    • 5144233105 scopus 로고
    • MLEV-17-based 2D homonuclear magnetization transfer spectroscopy
    • Bax, A. & Davis, D. G. (1985). MLEV-17-based 2D homonuclear magnetization transfer spectroscopy J. Magn. Reson. 65, 355-360.
    • (1985) J. Magn. Reson. , vol.65 , pp. 355-360
    • Bax, A.1    Davis, D.G.2
  • 2
    • 0019005874 scopus 로고
    • Determination of protein secondary structure in solution by vacuum ultraviolet circular dichroism
    • Brahms, S. & Brahms, J. (1980). Determination of protein secondary structure in solution by vacuum ultraviolet circular dichroism. J. Mol. Biol. 138, 149-178.
    • (1980) J. Mol. Biol. , vol.138 , pp. 149-178
    • Brahms, S.1    Brahms, J.2
  • 3
    • 0023372284 scopus 로고
    • Cap Z(36/32), a barbed end actin-capping protein, is a component of the Z-line of skeletal muscle
    • Casella, J. F., Craig, S. W., Maack, D. J. & Brown, A. E. (1987). Cap Z(36/32), a barbed end actin-capping protein, is a component of the Z-line of skeletal muscle. J. Cell Biol. 105, 371-379.
    • (1987) J. Cell Biol. , vol.105 , pp. 371-379
    • Casella, J.F.1    Craig, S.W.2    Maack, D.J.3    Brown, A.E.4
  • 4
    • 0028279663 scopus 로고
    • Conformational studies of a two-module fragment of nebulin and implications for actin association
    • Chen, M.-J. G. & Wang, K. (1994). Conformational studies of a two-module fragment of nebulin and implications for actin association. Arch. Biochem. Biophys. 310, 310-317.
    • (1994) Arch. Biochem. Biophys. , vol.310 , pp. 310-317
    • Chen, M.-J.G.1    Wang, K.2
  • 5
    • 0242554041 scopus 로고
    • Nebulin is an actin-binding, length regulating template protein of the thin filaments of skeletal muscle: Actin-interaction and confirmation of a two module human nebulin fragment
    • Chen, M.-J. G., Shih, C.-L., and Wang, K. (1993a). Nebulin is an actin-binding, length regulating template protein of the thin filaments of skeletal muscle: actin-interaction and confirmation of a two module human nebulin fragment. Biophys. J. 64, 147-159.
    • (1993) Biophys. J. , vol.64 , pp. 147-159
    • Chen, M.-J.G.1    Shih, C.-L.2    Wang, K.3
  • 7
    • 0015230487 scopus 로고
    • Determination of secondary structure of polypeptides in solution
    • Chen, Y. H. & Yang, Y. T. (1971). Determination of secondary structure of polypeptides in solution. Biochem. Biophys. Res. Commun. 44, 1285-1291.
    • (1971) Biochem. Biophys. Res. Commun. , vol.44 , pp. 1285-1291
    • Chen, Y.H.1    Yang, Y.T.2
  • 8
    • 0029077857 scopus 로고
    • Interactions between hydrophobic side chains within α-helices
    • Creamer, T. P. & Rose, G. D. (1995). Interactions between hydrophobic side chains within α-helices. Protein Sci. 4, 1305-1314.
    • (1995) Protein Sci. , vol.4 , pp. 1305-1314
    • Creamer, T.P.1    Rose, G.D.2
  • 10
    • 0024278572 scopus 로고
    • Folding of immunogenic peptide fragments of proteins in water solution. II. The nascent helix
    • Dyson, H. J., Rance, M., Houghten, R. A., Wright, P. E. & Lerner, R. A. (1988). Folding of immunogenic peptide fragments of proteins in water solution. II. The nascent helix. J. Mol. Biol. 201, 201-217.
    • (1988) J. Mol. Biol. , vol.201 , pp. 201-217
    • Dyson, H.J.1    Rance, M.2    Houghten, R.A.3    Wright, P.E.4    Lerner, R.A.5
  • 11
    • 0026768829 scopus 로고
    • Folding of peptide fragments comprising the complete sequence of proteins. Models for initiation of protein folding II. Myohemerythrin
    • Dyson, H. J., Merutka, G., Waltho, J. P., Lerner, R. A. & Wright, P. E. (1992). Folding of peptide fragments comprising the complete sequence of proteins. Models for initiation of protein folding II. Myohemerythrin. J. Mol. Biol. 226, 795-817.
    • (1992) J. Mol. Biol. , vol.226 , pp. 795-817
    • Dyson, H.J.1    Merutka, G.2    Waltho, J.P.3    Lerner, R.A.4    Wright, P.E.5
  • 12
    • 0019519177 scopus 로고
    • Phalloidin influence on F-actin stability
    • Ester, J. E., Selden, L. A., and Gershman, L. C. (1981). Phalloidin influence on F-actin stability Biochemistry, 20, 708-712.
    • (1981) Biochemistry , vol.20 , pp. 708-712
    • Ester, J.E.1    Selden, L.A.2    Gershman, L.C.3
  • 14
    • 0024382293 scopus 로고
    • Huge proteins in vertebrate striated muscle
    • Hu, D. H., Kimura, S. & Maruyama, K. (1989). Huge proteins in vertebrate striated muscle. Biomed. Res. 10, 165-171.
    • (1989) Biomed. Res. , vol.10 , pp. 165-171
    • Hu, D.H.1    Kimura, S.2    Maruyama, K.3
  • 15
    • 0027475153 scopus 로고
    • Helical peptides with three pairs of Asp-Arg and Glu-Arg residues in different orientations and spacings
    • Huyghues-Despointes, B. M. P., Scholtz, J. M. & Baldwin, R. L. (1993). Helical peptides with three pairs of Asp-Arg and Glu-Arg residues in different orientations and spacings. Protein Sci. 2, 80-85.
    • (1993) Protein Sci. , vol.2 , pp. 80-85
    • Huyghues-Despointes, B.M.P.1    Scholtz, J.M.2    Baldwin, R.L.3
  • 16
    • 0025840415 scopus 로고
    • Cloning, expression and protein interaction of human nebulin fragments composed of varying numbers of sequence modules
    • Jin, J.-P. & Wang, K. (1991a). Cloning, expression and protein interaction of human nebulin fragments composed of varying numbers of sequence modules. J. Biol. Chem. 266, 21215-21223.
    • (1991) J. Biol. Chem. , vol.266 , pp. 21215-21223
    • Jin, J.-P.1    Wang, K.2
  • 17
    • 0026101389 scopus 로고
    • Nebulin as a giant actin-binding template protein in skeletal muscle sarcomere
    • Jin, J.-P. & Wang, K. (1991b). Nebulin as a giant actin-binding template protein in skeletal muscle sarcomere. FEBS Letters, 281, 93.
    • (1991) FEBS Letters , vol.281 , pp. 93
    • Jin, J.-P.1    Wang, K.2
  • 18
    • 0028955760 scopus 로고
    • Structure and function of titin and nebulin
    • Keller, T. C. S. (1995). Structure and function of titin and nebulin. Curr. Biol. 7, 32-36.
    • (1995) Curr. Biol. , vol.7 , pp. 32-36
    • Keller, T.C.S.1
  • 19
    • 0026008748 scopus 로고
    • Nebulin as a length regulator of thin filaments of vertebrate skeletal muscles: Correlation of thin filament length, nebulin size and epitope profile
    • Kruger, M., Wright, J. & Wang, K. (1991). Nebulin as a length regulator of thin filaments of vertebrate skeletal muscles: correlation of thin filament length, nebulin size and epitope profile. J. Cell Biol. 115, 97-107.
    • (1991) J. Cell Biol. , vol.115 , pp. 97-107
    • Kruger, M.1    Wright, J.2    Wang, K.3
  • 20
    • 0029037896 scopus 로고
    • The complete primary structure of human nebulin and its correlation to muscle structure
    • Labeit, S. & Kolmerer, B. (1995). The complete primary structure of human nebulin and its correlation to muscle structure. J. Mol. Biol. 248, 308-315.
    • (1995) J. Mol. Biol. , vol.248 , pp. 308-315
    • Labeit, S.1    Kolmerer, B.2
  • 22
    • 0028101984 scopus 로고
    • Sequential appearance of muscle-specific proteins in myoblasts as a function of time after cell division: Evidence for a conserved myoblast differentiation program in skeletal muscle
    • Lin, Z., Lu, M. H., Schultheiss, T., Choi, J., DiLullo, S. H. C., Fischman, D. A. & Holtzer, H. (1994). Sequential appearance of muscle-specific proteins in myoblasts as a function of time after cell division: evidence for a conserved myoblast differentiation program in skeletal muscle. Cell Motil. Cytoskel. 29, 1-19.
    • (1994) Cell Motil. Cytoskel. , vol.29 , pp. 1-19
    • Lin, Z.1    Lu, M.H.2    Schultheiss, T.3    Choi, J.4    DiLullo, S.H.C.5    Fischman, D.A.6    Holtzer, H.7
  • 23
    • 0027131941 scopus 로고
    • Refinement of the F-actin model against X-ray fiber diffraction data by the use of a directed mutation algorithm
    • Lorenz, M., Popp, D. & Holmes, K. C. (1993). Refinement of the F-actin model against X-ray fiber diffraction data by the use of a directed mutation algorithm. J. Mol. Biol. 234, 452-463.
    • (1993) J. Mol. Biol. , vol.234 , pp. 452-463
    • Lorenz, M.1    Popp, D.2    Holmes, K.C.3
  • 24
    • 0018934798 scopus 로고
    • Viscometric analysis of the gelation of Acanthamoeba extracts and purification of two gelation factors
    • MacLean-Fletcher, S. D. & Pollard, T. D. (1980). Viscometric analysis of the gelation of Acanthamoeba extracts and purification of two gelation factors. J. Cell Biol. 85, 414-428.
    • (1980) J. Cell Biol. , vol.85 , pp. 414-428
    • MacLean-Fletcher, S.D.1    Pollard, T.D.2
  • 27
    • 0028784365 scopus 로고
    • Nebulette, a 107 kD nebulin-like protein in cardiac muscle
    • Moncman, C. L. & Wang, K. (1995). Nebulette, a 107 kD nebulin-like protein in cardiac muscle. Cell Mot. Cytoskel. 32, 205-225.
    • (1995) Cell Mot. Cytoskel. , vol.32 , pp. 205-225
    • Moncman, C.L.1    Wang, K.2
  • 28
    • 0028447768 scopus 로고
    • Elucidating the folding problem of helical peptides using empirical parameters
    • Munoz, V. & Serrano, L. (1994). Elucidating the folding problem of helical peptides using empirical parameters. Nature: Struct. Biol. 1, 399-409.
    • (1994) Nature: Struct. Biol. , vol.1 , pp. 399-409
    • Munoz, V.1    Serrano, L.2
  • 29
    • 0028873081 scopus 로고
    • Elucidating the folding problem of helical peptides using empirical parameters II. Helix macrodipole effects and rational modification of the helical content of natural peptides
    • Munoz, V. & Serrano, L. (1995). Elucidating the folding problem of helical peptides using empirical parameters II. Helix macrodipole effects and rational modification of the helical content of natural peptides. J. Mol. Biol. 245, 275-287.
    • (1995) J. Mol. Biol. , vol.245 , pp. 275-287
    • Munoz, V.1    Serrano, L.2
  • 30
    • 0025100156 scopus 로고
    • Interaction of alpha-actinin and nebulin in vitro. Support for the existence of a fourth filament system in skeletal muscle
    • Nave, R., Fürst, D. O. & Weber, K. (1990). Interaction of alpha-actinin and nebulin in vitro. Support for the existence of a fourth filament system in skeletal muscle. FEBS Letters, 269, 163-166.
    • (1990) FEBS Letters , vol.269 , pp. 163-166
    • Nave, R.1    Fürst, D.O.2    Weber, K.3
  • 31
    • 0028569692 scopus 로고
    • Tests for helix-stabilising interactions between various non-polar side chains in alanine based peptides
    • Padmanabhan, S. & Baldwin, R. L. (1994). Tests for helix-stabilising interactions between various non-polar side chains in alanine based peptides. Protein Sci. 3, 1992-1997.
    • (1994) Protein Sci. , vol.3 , pp. 1992-1997
    • Padmanabhan, S.1    Baldwin, R.L.2
  • 32
    • 0028347405 scopus 로고
    • Nebulin, a helical actin binding protein
    • Pfuhl, M., Winder, S. J., and Pastore, A. (1994). Nebulin, a helical actin binding protein. EMBO J. 13, 1782-1789.
    • (1994) EMBO J. , vol.13 , pp. 1782-1789
    • Pfuhl, M.1    Winder, S.J.2    Pastore, A.3
  • 33
    • 0028080839 scopus 로고
    • Calmodulin-sensitive interaction of human nebulin fragments with actin and myosin
    • Root, D. D. & Wang, K. (1994). Calmodulin-sensitive interaction of human nebulin fragments with actin and myosin. Biochemistry, 33, 12581-12591.
    • (1994) Biochemistry , vol.33 , pp. 12581-12591
    • Root, D.D.1    Wang, K.2
  • 34
    • 0025865320 scopus 로고
    • Solution structure of the basic region from the transcriptional activator GCN4
    • Saudek, V., Pasley H. S., Gibson, T., Gausepohl, H., Frank, R. & Pastore, A. (1990). Solution structure of the basic region from the transcriptional activator GCN4. Biochemistry, 31, 1310-1317.
    • (1990) Biochemistry , vol.31 , pp. 1310-1317
    • Saudek, V.1    Pasley, H.S.2    Gibson, T.3    Gausepohl, H.4    Frank, R.5    Pastore, A.6
  • 35
    • 0542406203 scopus 로고
    • Stabilisation of the long central helix of troponin C by intrahelical salt bridges between charged amino acid side chains
    • Sundaralingam, M., Drendel, W. & Greaser, M. (1985). Stabilisation of the long central helix of troponin C by intrahelical salt bridges between charged amino acid side chains. Proc. Natl Acad. Sci. USA, 82, 7944-7947.
    • (1985) Proc. Natl Acad. Sci. USA , vol.82 , pp. 7944-7947
    • Sundaralingam, M.1    Drendel, W.2    Greaser, M.3
  • 36
    • 0027968068 scopus 로고
    • Clustal W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson, J. D., Higgins, D. G. & Gibson, T. J. (1994). Clustal W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucl. Acids Res. 22, 4673-4680.
    • (1994) Nucl. Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 37
    • 0028091960 scopus 로고
    • Titin and nebulin: Protein rulers in muscle?
    • Trinick, J. (1994). Titin and nebulin: protein rulers in muscle? Trends. Biochem. Sci. 19, 405-409.
    • (1994) Trends. Biochem. Sci. , vol.19 , pp. 405-409
    • Trinick, J.1
  • 38
    • 0028102849 scopus 로고
    • Effect of conformational flexibility and solvation on receptor-ligand binding free energies
    • Vajda, S., Weng, Z., Rosenfeld, R. & DeLisi, C. (1994). Effect of conformational flexibility and solvation on receptor-ligand binding free energies. Biochemistry, 33, 13977-13988.
    • (1994) Biochemistry , vol.33 , pp. 13977-13988
    • Vajda, S.1    Weng, Z.2    Rosenfeld, R.3    DeLisi, C.4
  • 40
    • 0020012724 scopus 로고
    • Purification of titin and nebulin
    • Wang, K. (1982). Purification of titin and nebulin. Methods Enzymol. 85, 264-266.
    • (1982) Methods Enzymol. , vol.85 , pp. 264-266
    • Wang, K.1
  • 41
    • 0019028451 scopus 로고
    • Identification of a N2 line protein of striated muscle
    • Wang, K. & Williamson, C. (1980). Identification of a N2 line protein of striated muscle. Proc. Natl Acad. Sci. USA, 77, 3254-3258.
    • (1980) Proc. Natl Acad. Sci. USA , vol.77 , pp. 3254-3258
    • Wang, K.1    Williamson, C.2
  • 42
    • 0018324977 scopus 로고
    • Equilibrium of the actin-tropomyosin interaction
    • Wegner, A. (1979). Equilibrium of the actin-tropomyosin interaction. J. Mol. Biol. 131, 839-853.
    • (1979) J. Mol. Biol. , vol.131 , pp. 839-853
    • Wegner, A.1
  • 45
    • 0027331352 scopus 로고
    • Nebulin is a full-length template of actin filaments in the skeletal muscle sarcomere: An immunoelectron microscopic study of its orientation and span with site specific monoclonal antibodies
    • Wright, J., Huang, Q.-Q. & Wang, K. (1993). Nebulin is a full-length template of actin filaments in the skeletal muscle sarcomere: an immunoelectron microscopic study of its orientation and span with site specific monoclonal antibodies. J. Muscle Res. Cell. Motil. 14, 476-483.
    • (1993) J. Muscle Res. Cell. Motil. , vol.14 , pp. 476-483
    • Wright, J.1    Huang, Q.-Q.2    Wang, K.3
  • 46
    • 0026609553 scopus 로고
    • The two-stranded α-helical coiled-coil is an ideal model for studying protein stability and subunit interactions
    • Zhou, N. E., Zhu, B.-Y., May, C. M. & Hodges, R. S. (1992). The two-stranded α-helical coiled-coil is an ideal model for studying protein stability and subunit interactions. Biopolymers, 32, 419-426.
    • (1992) Biopolymers , vol.32 , pp. 419-426
    • Zhou, N.E.1    Zhu, B.-Y.2    May, C.M.3    Hodges, R.S.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.