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Volumn 26, Issue 2, 1996, Pages 134-145

Heptad breaks in α-helical coiled coils: Stutters and stammers

Author keywords

fibrous proteins; hemagglutinin; mannose binding protein; protein engineering; structure prediction; supercoiling

Indexed keywords

HEMAGGLUTININ; MANNOSE BINDING PROTEIN; MYOSIN;

EID: 0029957901     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-0134(199610)26:2<134::AID-PROT3>3.0.CO;2-G     Document Type: Article
Times cited : (246)

References (57)
  • 1
    • 0026331267 scopus 로고
    • X-ray structure of the GCN4 leucine zipper, a two-stranded, parallel coiled coil
    • O'Shea, E.K., Klemm, J.D., Kim, P.S., Alber, T. X-ray structure of the GCN4 leucine zipper, a two-stranded, parallel coiled coil. Science 254:539-544, 1991.
    • (1991) Science , vol.254 , pp. 539-544
    • O'Shea, E.K.1    Klemm, J.D.2    Kim, P.S.3    Alber, T.4
  • 2
    • 0027756896 scopus 로고
    • A switch between two-, three- and four-stranded coiled coils in GCN4 leucine zipper mutants
    • Harbury, P.B., Zhang, T., Kim, P.S., Alber, T. A switch between two-, three- and four-stranded coiled coils in GCN4 leucine zipper mutants. Science 262:1401-1407, 1993.
    • (1993) Science , vol.262 , pp. 1401-1407
    • Harbury, P.B.1    Zhang, T.2    Kim, P.S.3    Alber, T.4
  • 3
    • 0027934571 scopus 로고
    • Crystal structure of an isoleucine-zipper trimer
    • Harbury, P.B., Kim, P.S., Alber, T. Crystal structure of an isoleucine-zipper trimer. Nature 371:80-83, 1994.
    • (1994) Nature , vol.371 , pp. 80-83
    • Harbury, P.B.1    Kim, P.S.2    Alber, T.3
  • 4
    • 0026028894 scopus 로고
    • Three-stranded α-fibrous proteins: The heptad repeat and its implications for structure
    • Conway, J.F., Parry, D.A.D. Three-stranded α-fibrous proteins: The heptad repeat and its implications for structure. Int. J. Biol. Macromol. 13:14-16, 1991.
    • (1991) Int. J. Biol. Macromol. , vol.13 , pp. 14-16
    • Conway, J.F.1    Parry, D.A.D.2
  • 5
    • 0002732819 scopus 로고
    • Compound helical configurations of polypeptide chains: Structure of proteins of the α-keratin type
    • Pauling, L., Corey, R.B. Compound helical configurations of polypeptide chains: Structure of proteins of the α-keratin type. Nature 171:59-61, 1953.
    • (1953) Nature , vol.171 , pp. 59-61
    • Pauling, L.1    Corey, R.B.2
  • 6
    • 0025272940 scopus 로고
    • α-helical coiled coils and bundles: How to design an α-helical protein
    • Cohen, C., Parry, D.A.D. α-helical coiled coils and bundles: How to design an α-helical protein. Proteins 7:1-15, 1990.
    • (1990) Proteins , vol.7 , pp. 1-15
    • Cohen, C.1    Parry, D.A.D.2
  • 7
    • 0000920828 scopus 로고
    • The packing of α-helices: Simple coiled coils
    • Crick, F.H.C. The packing of α-helices: Simple coiled coils. Acta Crystallogr. 6:689-697, 1953.
    • (1953) Acta Crystallogr. , vol.6 , pp. 689-697
    • Crick, F.H.C.1
  • 8
    • 0028987628 scopus 로고
    • Model structure of the Ompα rod, a parallel four-stranded coiled coil from the hyperthermophilic eubacterium Thermotoga maritima
    • Lupas, A. Müller, S., Goldie, K., Engel, A.M., Engel, A., Baumeister, W. Model structure of the Ompα rod, a parallel four-stranded coiled coil from the hyperthermophilic eubacterium Thermotoga maritima. J. Mol. Biol. 248:180-189, 1995.
    • (1995) J. Mol. Biol. , vol.248 , pp. 180-189
    • Lupas, A.1    Müller, S.2    Goldie, K.3    Engel, A.M.4    Engel, A.5    Baumeister, W.6
  • 9
    • 0017849653 scopus 로고
    • Fibrinogen: A preliminary analysis of the amino acid sequences of the portions of the α,β, and γ-chains postulated to form the interdomainal link between globular regions of the molecule
    • Parry, D.A.D. Fibrinogen: A preliminary analysis of the amino acid sequences of the portions of the α,β, and γ-chains postulated to form the interdomainal link between globular regions of the molecule. J. Mol. Biol. 120: 545-551, 1978.
    • (1978) J. Mol. Biol. , vol.120 , pp. 545-551
    • Parry, D.A.D.1
  • 11
    • 0023915219 scopus 로고
    • Structure of the influenza virus haemagglutinin complexed with its receptor, sialic acid
    • Weis, W., Brown, J.H., Cusack, S., Paulson, J.C., Skehel, J.J., Wiley, D.C. Structure of the influenza virus haemagglutinin complexed with its receptor, sialic acid. Nature 333:426-431, 1988.
    • (1988) Nature , vol.333 , pp. 426-431
    • Weis, W.1    Brown, J.H.2    Cusack, S.3    Paulson, J.C.4    Skehel, J.J.5    Wiley, D.C.6
  • 12
    • 0019890491 scopus 로고
    • Structure of the haemagglutinin membrane glycoprotein of influenza virus at 3 Å resolution
    • Wilson, I.A., Skehel, J.J., Wiley, D.C. Structure of the haemagglutinin membrane glycoprotein of influenza virus at 3 Å resolution. Nature 289:366-373, 1981.
    • (1981) Nature , vol.289 , pp. 366-373
    • Wilson, I.A.1    Skehel, J.J.2    Wiley, D.C.3
  • 13
    • 0027949066 scopus 로고
    • Coiled-coil stutter and link segments in keratin and other intermediate filament molecules: A computer modeling study
    • North, A.C.T., Steinert, P.M., Parry, D.A.D. Coiled-coil stutter and link segments in keratin and other intermediate filament molecules: A computer modeling study. Proteins 20:174-184, 1994.
    • (1994) Proteins , vol.20 , pp. 174-184
    • North, A.C.T.1    Steinert, P.M.2    Parry, D.A.D.3
  • 14
    • 0020620928 scopus 로고
    • Protein structural domains in the Caenorhabditis elegans une- 54 myosin heavy chain gene are not separated by introns
    • Karn, J., Brenner, S., Barnett, L. Protein structural domains in the Caenorhabditis elegans une- 54 myosin heavy chain gene are not separated by introns. Proc. Natl. Acad. Sci. U.S.A. 80:4253-4257, 1983.
    • (1983) Proc. Natl. Acad. Sci. U.S.A. , vol.80 , pp. 4253-4257
    • Karn, J.1    Brenner, S.2    Barnett, L.3
  • 15
    • 0024974671 scopus 로고
    • The paramyosin gene (unc-15) of Caenorhabditis elegans: Molecular cloning nucleotide sequence and models for thick filament assembly
    • Kagawa, H., Gengyo, K., McLachlan, A.D., Brenner, S., Karn, J. The paramyosin gene (unc-15) of Caenorhabditis elegans: Molecular cloning nucleotide sequence and models for thick filament assembly. J. Mol. Biol. 207:311-333, 1989.
    • (1989) J. Mol. Biol. , vol.207 , pp. 311-333
    • Kagawa, H.1    Gengyo, K.2    McLachlan, A.D.3    Brenner, S.4    Karn, J.5
  • 16
    • 0020171992 scopus 로고
    • Protein chemical characterization of three structurally distinct domains along the protofilament unit of desmin 10 nm filaments
    • Geisler, N., Kaufman, E., Weber, K. Protein chemical characterization of three structurally distinct domains along the protofilament unit of desmin 10 nm filaments. Cell 30:277-286, 1982.
    • (1982) Cell , vol.30 , pp. 277-286
    • Geisler, N.1    Kaufman, E.2    Weber, K.3
  • 18
    • 0025743954 scopus 로고
    • Comparison of molecularly cloned bullous pemphigoid antigen to desmoplakin I confirms that they define a new family of cell adhesion junction plaque proteins
    • Tanaka, T., Parry, D.A.D., Klaus-Kovtun, V., Steinert, P.M., Stanley, J.R. Comparison of molecularly cloned bullous pemphigoid antigen to desmoplakin I confirms that they define a new family of cell adhesion junction plaque proteins. J. Biol. Chem. 266:12555-12559, 1991.
    • (1991) J. Biol. Chem. , vol.266 , pp. 12555-12559
    • Tanaka, T.1    Parry, D.A.D.2    Klaus-Kovtun, V.3    Steinert, P.M.4    Stanley, J.R.5
  • 19
    • 0026014584 scopus 로고
    • Cloning and sequencing of rat plectin indicates a 466 kD polypeptide chain with a three-domain structure based on a central alpha-helical coiled coil
    • Wiche, G., Becker, B., Luber, K., Weitzer, G., Castanon, M.J., Hauptaman, R., Stratowa, C., Stewart, M. Cloning and sequencing of rat plectin indicates a 466 kD polypeptide chain with a three-domain structure based on a central alpha-helical coiled coil. J. Cell Biol. 114:83-99, 1991.
    • (1991) J. Cell Biol. , vol.114 , pp. 83-99
    • Wiche, G.1    Becker, B.2    Luber, K.3    Weitzer, G.4    Castanon, M.J.5    Hauptaman, R.6    Stratowa, C.7    Stewart, M.8
  • 22
    • 0028022979 scopus 로고
    • NuMa/centrophilin: Sequence analysis of the coiled-coil rod domain
    • Parry, D.A.D. NuMa/centrophilin: Sequence analysis of the coiled-coil rod domain. Biophys. J. 67:1203-1206, 1994.
    • (1994) Biophys. J. , vol.67 , pp. 1203-1206
    • Parry, D.A.D.1
  • 23
    • 0026588744 scopus 로고
    • The NUF1 gene encodes an essential coiled-coil related protein that is a potential component of the yeast nucleoskeleton
    • Mirzayan, C., Copeland, C.S., Snyder, M. The NUF1 gene encodes an essential coiled-coil related protein that is a potential component of the yeast nucleoskeleton. J. Cell Biol. 116:1319-1332, 1992.
    • (1992) J. Cell Biol. , vol.116 , pp. 1319-1332
    • Mirzayan, C.1    Copeland, C.S.2    Snyder, M.3
  • 24
    • 0028298370 scopus 로고
    • Nuf2, a spindle pole body-associated protein required for nuclear division in yeast
    • Osborne, M.A., Schlenstedt, G., Jinks, T., Silver, P.A. Nuf2, a spindle pole body-associated protein required for nuclear division in yeast. J. Cell Biol. 125:853-866, 1994.
    • (1994) J. Cell Biol. , vol.125 , pp. 853-866
    • Osborne, M.A.1    Schlenstedt, G.2    Jinks, T.3    Silver, P.A.4
  • 25
    • 0026743913 scopus 로고
    • CIK1: A developmentally regulated spindle pole body-associated protein important for microtubule function in Saccharomyces cerevisiae
    • Page, B.D., Snyder, M. CIK1: A developmentally regulated spindle pole body-associated protein important for microtubule function in Saccharomyces cerevisiae. Gene Dev. 6:1414-1429, 1992.
    • (1992) Gene Dev. , vol.6 , pp. 1414-1429
    • Page, B.D.1    Snyder, M.2
  • 26
    • 0025239030 scopus 로고
    • The primary structure and analysis of the squid kinesin heavy chain
    • Kosik, K.S., Orecchio, L.D., Schnapp, B., Inouye, H., Neve, R.L. The primary structure and analysis of the squid kinesin heavy chain. J. Biol. Chem. 265:3278-3283, 1990.
    • (1990) J. Biol. Chem. , vol.265 , pp. 3278-3283
    • Kosik, K.S.1    Orecchio, L.D.2    Schnapp, B.3    Inouye, H.4    Neve, R.L.5
  • 27
    • 0024431099 scopus 로고
    • Isolation of dynein heavy chain cDNAs from trout testis which predict an extensive carboxyl-terminal alpha-helical coiled-coil domain
    • Garber, A.T., Retief, J.D., Dixon, G.H. Isolation of dynein heavy chain cDNAs from trout testis which predict an extensive carboxyl-terminal alpha-helical coiled-coil domain. EMBO J. 8:1727-1734, 1989.
    • (1989) EMBO J. , vol.8 , pp. 1727-1734
    • Garber, A.T.1    Retief, J.D.2    Dixon, G.H.3
  • 28
    • 0028218025 scopus 로고
    • Pericentrin, a highly conserved centrosome protein involved in microtubule organization
    • Doxsey, S.J., Stein, P., Evans, L., Calarco P.D., Kirschner, M. Pericentrin, a highly conserved centrosome protein involved in microtubule organization. Cell 76:639-650, 1994.
    • (1994) Cell , vol.76 , pp. 639-650
    • Doxsey, S.J.1    Stein, P.2    Evans, L.3    Calarco, P.D.4    Kirschner, M.5
  • 29
    • 0027167511 scopus 로고
    • SF-assemblin, the structural protein of the 2-nm filaments from striated microtubule associated fibers of algal flagellar roots, forms a segmented coiled coil
    • Weber, K., Geisler, N., Plessmann, U., Bremerich, A., Lechtreck, K-F., Melkonian, M. SF-assemblin, the structural protein of the 2-nm filaments from striated microtubule associated fibers of algal flagellar roots, forms a segmented coiled coil. J. Cell Biol. 121:837-845, 1993.
    • (1993) J. Cell Biol. , vol.121 , pp. 837-845
    • Weber, K.1    Geisler, N.2    Plessmann, U.3    Bremerich, A.4    Lechtreck, K.-F.5    Melkonian, M.6
  • 30
    • 0027519779 scopus 로고
    • Novel heterotrimeric kinesin-related protein purified from sea urchin eggs
    • Cole, D.G., Chinn, S.W., Wedaman, K.P., Hall, K., Vuong, T., Scholey, J.M. Novel heterotrimeric kinesin-related protein purified from sea urchin eggs. Nature 366:268-270, 1993.
    • (1993) Nature , vol.366 , pp. 268-270
    • Cole, D.G.1    Chinn, S.W.2    Wedaman, K.P.3    Hall, K.4    Vuong, T.5    Scholey, J.M.6
  • 31
    • 0024279637 scopus 로고
    • Segmented α-helical coiled-coil structure of the protein giardin from the giardia cytoskeleton
    • Holberton, D., Baker, D.A., Marshall, J. Segmented α-helical coiled-coil structure of the protein giardin from the giardia cytoskeleton. J. Mol. Biol. 204:789-795, 1988.
    • (1988) J. Mol. Biol. , vol.204 , pp. 789-795
    • Holberton, D.1    Baker, D.A.2    Marshall, J.3
  • 32
    • 0027157011 scopus 로고
    • Sequence and structure of a new coiled-coil protein from a microtubule bundle in giardia
    • Marshall, J., Holberton, D.V. Sequence and structure of a new coiled-coil protein from a microtubule bundle in giardia. J. Mol. Biol. 231:521-530, 1993.
    • (1993) J. Mol. Biol. , vol.231 , pp. 521-530
    • Marshall, J.1    Holberton, D.V.2
  • 33
    • 0029099085 scopus 로고
    • Giardia gene predicts a 183 kDa nucleotide-binding head-stalk protein
    • Marshall, J., Holberton, D.V. Giardia gene predicts a 183 kDa nucleotide-binding head-stalk protein. J. Cell Sci. 108:2683-2692, 1995.
    • (1995) J. Cell Sci. , vol.108 , pp. 2683-2692
    • Marshall, J.1    Holberton, D.V.2
  • 34
    • 0025336325 scopus 로고
    • Sec2 protein contains a coiled-coil domain essential for vesicular transport and a dispensable carboxy terminal domain
    • Nair, J., Müller, H. Peterson, M. and Novick, P. Sec2 protein contains a coiled-coil domain essential for vesicular transport and a dispensable carboxy terminal domain. J. Cell Biol. 110:1897-1909, 1990.
    • (1990) J. Cell Biol. , vol.110 , pp. 1897-1909
    • Nair, J.1    Müller, H.2    Peterson, M.3    Novick, P.4
  • 35
    • 0027759461 scopus 로고
    • SMCI: An essential yeast gene encoding a putative head-rod-tail protein is required for nuclear division and defines a new ubiquitous protein family
    • Strunnikov, A.V., Larionov, V.L., Koshland, D. SMCI: An essential yeast gene encoding a putative head-rod-tail protein is required for nuclear division and defines a new ubiquitous protein family. J. Cell Biol. 123:1635-1648, 1993.
    • (1993) J. Cell Biol. , vol.123 , pp. 1635-1648
    • Strunnikov, A.V.1    Larionov, V.L.2    Koshland, D.3
  • 36
    • 0025852462 scopus 로고
    • The Wac gene product of bacteriophage T4 contains coiled-coil structural patterns
    • Sobolev, B.N., Mesyanzhinov, V.V. The Wac gene product of bacteriophage T4 contains coiled-coil structural patterns. J. Biomol. Struct. Dynamics 8:953-965, 1991.
    • (1991) J. Biomol. Struct. Dynamics , vol.8 , pp. 953-965
    • Sobolev, B.N.1    Mesyanzhinov, V.V.2
  • 37
    • 0025372616 scopus 로고
    • Molecular structure of the cell-attachment protein of reovirus: Correlation of computer-processed electron micrographs with sequence-based predictions
    • Fraser, R.D.B., Furlong, D.B., Trus, B.L., Nibert, M.L., Fields, B.N., Steven, A.C. Molecular structure of the cell-attachment protein of reovirus: Correlation of computer-processed electron micrographs with sequence-based predictions. J. Virol. 64:2990-3000, 1990.
    • (1990) J. Virol. , vol.64 , pp. 2990-3000
    • Fraser, R.D.B.1    Furlong, D.B.2    Trus, B.L.3    Nibert, M.L.4    Fields, B.N.5    Steven, A.C.6
  • 39
    • 0025805962 scopus 로고
    • A cytoskeleton-related gene, USO1, is required for intracellular protein transport in Saccharomyces cerevisiae
    • Nakajima, H., Hirata, A., Ogawa, Y., Yonehara, T., Yoda, K., Yamasaki, M. A cytoskeleton-related gene, USO1, is required for intracellular protein transport in Saccharomyces cerevisiae. J. Cell Biol. 113:245-260, 1991.
    • (1991) J. Cell Biol. , vol.113 , pp. 245-260
    • Nakajima, H.1    Hirata, A.2    Ogawa, Y.3    Yonehara, T.4    Yoda, K.5    Yamasaki, M.6
  • 40
    • 10344223101 scopus 로고
    • submitted April Accession S43597
    • Ainscough, R. (submitted to EMBL Data Library, April 1994, Accession S43597).
    • (1994) EMBL Data Library
    • Ainscough, R.1
  • 41
    • 0024805562 scopus 로고
    • Structure of the Drosophila bicaudalD protein and its role in localizing the posterior determinant nanos
    • Wharton, R.P., Struhl, G. Structure of the Drosophila bicaudalD protein and its role in localizing the posterior determinant nanos. Cell 59:881-892, 1989.
    • (1989) Cell , vol.59 , pp. 881-892
    • Wharton, R.P.1    Struhl, G.2
  • 42
    • 0026439405 scopus 로고
    • The human tpr gene encodes a protein of 2094 amino acids that has extensive coiled-coil regions and an acidic C-terminal domain
    • Mitchell, P.J., Cooper, C.S. The human tpr gene encodes a protein of 2094 amino acids that has extensive coiled-coil regions and an acidic C-terminal domain. Oncogene 7:2329-2333, 1992.
    • (1992) Oncogene , vol.7 , pp. 2329-2333
    • Mitchell, P.J.1    Cooper, C.S.2
  • 43
    • 0027532105 scopus 로고
    • Pitch diversity in α-helical coiled coils
    • Seo, J., Cohen, C. Pitch diversity in α-helical coiled coils. Proteins 15:223-234, 1993.
    • (1993) Proteins , vol.15 , pp. 223-234
    • Seo, J.1    Cohen, C.2
  • 44
    • 0028840106 scopus 로고
    • Crystal structure of the GreA transcript cleavage factor from Escherichia coli
    • Stebbins, C.E., Borukhov, S., Orlova, M., Polyakov, A., Goldfarb, A., Darst, S.A. Crystal structure of the GreA transcript cleavage factor from Escherichia coli. Nature 373:636-640, 1995.
    • (1995) Nature , vol.373 , pp. 636-640
    • Stebbins, C.E.1    Borukhov, S.2    Orlova, M.3    Polyakov, A.4    Goldfarb, A.5    Darst, S.A.6
  • 45
    • 0028023726 scopus 로고
    • Structure of influenza haemagglutinin at the pH of membrane fusion
    • Bullough, P.A., Hughson, P.M. Skehel, J.J., Wiley, D.C. Structure of influenza haemagglutinin at the pH of membrane fusion. Nature 371:37-43, 1994.
    • (1994) Nature , vol.371 , pp. 37-43
    • Bullough, P.A.1    Hughson, P.M.2    Skehel, J.J.3    Wiley, D.C.4
  • 46
    • 0026463516 scopus 로고
    • What is the pitch of the α-helical coiled coil?
    • Phillips, G.N., Jr. What is the pitch of the α-helical coiled coil? Proteins 14:425-429, 1992.
    • (1992) Proteins , vol.14 , pp. 425-429
    • Phillips Jr., G.N.1
  • 47
    • 0028774718 scopus 로고
    • Trimeric structure of a C-type mannose-binding protein
    • Weis, W.I., Drickamer, K. Trimeric structure of a C-type mannose-binding protein. Structure 2:1227-1240, 1994.
    • (1994) Structure , vol.2 , pp. 1227-1240
    • Weis, W.I.1    Drickamer, K.2
  • 48
    • 0028533911 scopus 로고
    • Human mannosebinding protein carbohydrate recognition domain trimerizes through a triple α-helical coiled coil
    • Sheriff, S., Chang, C.Y., Ezekowitz, A.B. Human mannosebinding protein carbohydrate recognition domain trimerizes through a triple α-helical coiled coil. Struct. Biol. 1:789-793, 1994.
    • (1994) Struct. Biol. , vol.1 , pp. 789-793
    • Sheriff, S.1    Chang, C.Y.2    Ezekowitz, A.B.3
  • 49
    • 0026547747 scopus 로고
    • DNA recognition by GAL4: Structure of a protein-DNA complex
    • Marmorstein, R., Carey, M., Ptashne, M., Harrison, S.C. DNA recognition by GAL4: Structure of a protein-DNA complex. Nature 356:408-414, 1992.
    • (1992) Nature , vol.356 , pp. 408-414
    • Marmorstein, R.1    Carey, M.2    Ptashne, M.3    Harrison, S.C.4
  • 50
    • 0024290472 scopus 로고
    • Amino acid preferences for specific locations at the ends of α helices
    • Richardson, J.S., Richardson, D.C. Amino acid preferences for specific locations at the ends of α helices. Science 240: 1648-1652, 1988.
    • (1988) Science , vol.240 , pp. 1648-1652
    • Richardson, J.S.1    Richardson, D.C.2
  • 51
    • 0027253445 scopus 로고
    • A spring-loaded mechanism for the conformational change of influenza hemagglutinin
    • Carr, C.M., Kim, P.S. A spring-loaded mechanism for the conformational change of influenza hemagglutinin. Cell 73:823-832, 1993.
    • (1993) Cell , vol.73 , pp. 823-832
    • Carr, C.M.1    Kim, P.S.2
  • 52
    • 0019051305 scopus 로고
    • Influenza virus haemagglutinin: Structural predictions suggest that the fibrillar appearance is due to the presence of a coiled coil
    • Ward, C.W., Dopheide, T.A. Influenza virus haemagglutinin: Structural predictions suggest that the fibrillar appearance is due to the presence of a coiled coil. Aust. J. Biol. Sci. 33:441-447, 1980.
    • (1980) Aust. J. Biol. Sci. , vol.33 , pp. 441-447
    • Ward, C.W.1    Dopheide, T.A.2
  • 53
    • 0021103673 scopus 로고
    • Periodic features in the amino acid sequence of nematode myosin rod
    • McLachlan, A.D., Kara, J. Periodic features in the amino acid sequence of nematode myosin rod. J. Mol. Biol. 164: 605-626, 1983.
    • (1983) J. Mol. Biol. , vol.164 , pp. 605-626
    • McLachlan, A.D.1    Kara, J.2
  • 54
    • 0025601653 scopus 로고
    • Skip residues correlate with bends in the myosin tail
    • Offer, G. Skip residues correlate with bends in the myosin tail. J. Mol. Biol. 216:213-218, 1990.
    • (1990) J. Mol. Biol. , vol.216 , pp. 213-218
    • Offer, G.1
  • 55
    • 0028978047 scopus 로고
    • Computer Modelling of the α-helical coiled coil: Packing of side-chains in the inner core
    • Offer, G., Sessions, R. Computer Modelling of the α-helical coiled coil: Packing of side-chains in the inner core. J. Mol. Biol. 249:967-987, 1995.
    • (1995) J. Mol. Biol. , vol.249 , pp. 967-987
    • Offer, G.1    Sessions, R.2
  • 57
    • 0023042847 scopus 로고
    • Tropomyosin crystal structure and muscle regulation
    • Phillips, G.N., Jr., Fillers, J.P., Cohen, C. Tropomyosin crystal structure and muscle regulation. J. Mol. Biol. 192: 111-131, 1986.
    • (1986) J. Mol. Biol. , vol.192 , pp. 111-131
    • Phillips Jr., G.N.1    Fillers, J.P.2    Cohen, C.3


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