Structural Aspects of Intermediate Filaments

  • Norbert Geisler
  • Klaus Weber


Microtubules, microfilaments, and intermediate filaments (IF) form the three filamentous organizations of the cytoplasm. Whereas the major structural components of the two former systems—actin and tubulin—are highly conserved in different cell types, the constituent proteins of IF can vary greatly in amino acid sequence and length (40–200 K). This peculiar property led originally to much confusion as to the similarity and divergence of IF proteins. By the late 1970s it was obvious that IF proteins could be subdivided by biochemical and particularly by immunological data in a histologically meaningful manner as their expression pattern coincided with known rules of embryonic differentiation (for review see Lazarides, 1982; Osborn et al., 1982). Five subclasses were identified: epithelial keratins, neuronal neurofilaments, desmin filaments of most muscles, GFAP filaments of glia, and vimentin filaments present primarily in mesenchymal cells. Subsequent biochemical results documented around 20 different human keratins some of which were again markers of morphologically distinct epithelia (for review see Moll et al., 1982).


Intermediate Filament Intermediate Filament Protein Intermediate Filament Epidermal Keratin Chymotryptic Digestion 
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  1. Aebi, U., Fowler, W. E., Rew, P., and Sun, T. T., 1983, The fibrillar substructure of keratin filaments unraveled, J. Cell Biol 97: 1131.PubMedCrossRefGoogle Scholar
  2. Ahmadi, B., and Speakman, P. T., 1978, Suberimidate crosslinking shows that a rod shaped, low cystin, high helix protein prepared by limited proteolysis of reduced wool has four protein chains, FEBS Lett. 94: 365.PubMedCrossRefGoogle Scholar
  3. Ahmadi, B., Boston, N. M., Dobb, M. G., and Speakman, P. T., 1979, Possible four-chain repeating unit in the microfibril of wool, in: Fibrous Proteins (D. A. D. Parry, ed.), Vol. 2, pp. 161–166, Academic Press, New York.Google Scholar
  4. Chin, T. K., Eagles, P. A. M., and Maggs, A., 1983, The proteolytic digestion of ox-neurofllaments with trypsin and α-chymotrypsin, Biochem. J. 215: 239.PubMedGoogle Scholar
  5. Crewther, W. G., 1976, Primary structure and chemical properties of wool, in: Proceedings of the 5th International Wool Textile Research Conference, Aachen, 1975, Vol. 1, pp. 1 –101.Google Scholar
  6. Crewther, W. G., and Dowling, L. M., 1971, The preparation and properties of large peptides from the helical regions of low-sulphur proteins of wool, Appl. Polymer Symp. 18: 1–20.Google Scholar
  7. Crewther, W. G., Dowling, L. M., and Inglis, A. S., 1980, Amino acid sequence data from a microfibrillar protein of α-keratin, in: Proceedings of the 6th Quinquennial International Wool Textile Research Conference, Pretoria, Vol. 2, pp. 79–91.Google Scholar
  8. Crewther, W. G., Dowling, L. M., Steinert, P. M., and Parry, D. A. D., 1983, The structure of intermediate filaments, Int. J. Biol. Macromol. 5: 267.CrossRefGoogle Scholar
  9. Day, W. A., and Gilbert, D. S., 1972, X-ray diffraction pattern of axoplasm, Biochem. Biophys. Acta 285: 506.Google Scholar
  10. Debus, E., Weber, K., and Osborn, M., 1983, Monoclonal antibodies to desmin, the muscle- specific intermediate filament protein, EMBO J. 2: 2305.PubMedGoogle Scholar
  11. Dowling, L. M., Parry, D. A. D., and Sparrow, L. G., 1983, Structural homology between a- keratin and the intermediate filament proteins desmin and vimentin, Biosci. Rep. 3: 73.PubMedCrossRefGoogle Scholar
  12. Eagles, P. A. M., Gilbert, D. S., and Maggs, A., 1981, The polypeptide composition of axoplasm and of neurofilaments from the marine worm Myxicola infundibulum, Biochem. J. 199: 89.Google Scholar
  13. Franke, W. W., Schiller, D. L., Hatzfeld, R., and Winter, S., 1983, Protein complexes of intermediate-sized filaments: Melting of cytokeratin complexes in urea reveals different polypeptide separation characteristics, Proc. Natl. Acad. Sci. USA 80: 7113.PubMedCrossRefGoogle Scholar
  14. Fraser, R. D. B., and McRae, T. P., 1983, The structure of the a-keratin microfibril, Biosci. Rep. 3:517.Google Scholar
  15. Fraser, R. D. B., and McRae, T. P., 1983, The structure of the α-keratin microfibril, Biosci. Rep. 3: 517.PubMedCrossRefGoogle Scholar
  16. Fraser, R. D. B., and McRae, T. P., 1985, Biosci. Rep. 5: 573–579.PubMedCrossRefGoogle Scholar
  17. Fraser, R. D. B., McRae, T. P., and Suzuki, E., 1976, Structure of the a-keratin microfibril, J. Mol. Biol. 108: 435.PubMedCrossRefGoogle Scholar
  18. Fuchs, E., and Marchuk, D., 1983, Type I and type II keratins have evolved from lower eu- karyotes to form the epidermal intermediate filaments in mammalian skin, Proc. Natl. Acad. Sci. USA 80: 5857.PubMedCrossRefGoogle Scholar
  19. Gardner, E. E., Dahl, D., and Bignami, A., 1984, Formation of 10-nanometer filaments from the 150 K-Dalton neurofilament protein in vitro, J. Neurosci. Res. 11: 145.PubMedCrossRefGoogle Scholar
  20. Geisler, N., and Weber, K., 1981a, Selfassembly in vitro of the 68,000 molecular weight component of the mammalian neurofilament triplet proteins into intermediate-sized filaments, J. Mol. Biol. 151: 565.PubMedCrossRefGoogle Scholar
  21. Geisler, N., and Weber, K., 1981b, Comparison of the proteins of two immunologically distinct intermediate-sized filaments by amino acid sequence analysis: desmin and vimentin, Proc. Nat. Acad. Sci. USA 78: 4120.PubMedCrossRefGoogle Scholar
  22. Geisler, N., and Weber, K., 1982, The amino acid sequence of chicken muscle desmin provides a common structural model for intermediate filament proteins including the wool a-keratins, EMBO J. 1: 1649.PubMedGoogle Scholar
  23. Geisler, N., and Weber, K., 1983, Amino acid sequence data on glial fibrillary acidic protein (GFA); implications for the subdivision of intermediate filaments into epithelial and non- epithelial members, EMBO J. 2: 2059.PubMedGoogle Scholar
  24. Geisler, N., Kaufmann, E., and Weber, K., 1982a, Proteinchemical characterization of three structurally distinct domains along the protofilament unit of desmin 10 nm filaments, Cell 30: 277.PubMedCrossRefGoogle Scholar
  25. Geisler, N., Plessmann, U., and Weber, K., 1982b, Related amino acid sequences in neurofilaments and non neuronal intermediate filaments, Nature 296: 448.PubMedCrossRefGoogle Scholar
  26. Geisler, N., Kaufmann, E., Fischer, S., Plessmann, U., and Weber, K., 1983a, Neurofilament architecture combines structural principles of intermediate filaments with carboxy-terminal extensions increasing in size between triplet proteins, EMBO J. 2: 1295.PubMedGoogle Scholar
  27. Geisler, N., Plessmann, U., and Weber, K., 1983b, Amino acid sequence characterization of mammalian vimentin, the mesenchymal intermediate filament protein, FEBS Lett. 163: 22.PubMedCrossRefGoogle Scholar
  28. Geisler, N., Fischer, S., Vandekerckhove, J., Plessmann, U., and Weber, K., 1984, Hybrid character of a large neurofilament protein (NF-M): Intermediate filament type sequence followed by a long and acidic carboxy-terminal extension, EMBO J. 3: 2701.PubMedGoogle Scholar
  29. Geisler, N., Kaufmann, E., and Weber, K., 1985a, Antiparallel orientation of the two double- stranded coiled-coils in the tetrameric protofilament unit of intermediate filaments, J. Mol. Biol. 182: 173.PubMedCrossRefGoogle Scholar
  30. Geisler, N., Fischer, S., Vandekerckhove, J., Van Damme, J., Plessmann, U., and Weber, K., 1985b, Protein-chemical characterization of NF-H, the largest mammalian neurofilament component; intermediate filament-type sequences followed by a unique carboxy-terminal extension, EMBO J. 4: 57.PubMedGoogle Scholar
  31. Geisler, N., Plessmann, U., and Weber, K., 1985c, The complete amino acid sequence of the major mammalian neurofilament protein (NF-L), FEBS Lett. 182: 475.PubMedCrossRefGoogle Scholar
  32. Hanukoglu, I, and Fuchs, E., 1982, The CDNA sequence of a human epidermal keratin: divergence of sequence but conservation of structure among intermediate filament proteins, Cell 31: 243.PubMedCrossRefGoogle Scholar
  33. Hanukoglu, I., and Fuchs, E., 1983, The cDNA sequence of a type II cytoskeletal keratin reveals constant and variable structural domains among keratins, Cell 33: 915.PubMedCrossRefGoogle Scholar
  34. Henderson, D., Geisler, N., and Weber, K., 1982, A periodic ultrastructure in intermediate filaments, J. Mol Biol 155: 173.PubMedCrossRefGoogle Scholar
  35. Hirokawa, N., Glicksman, M. A., and Willard, M. B., 1984, Organization of mammalian neurofilament polypeptides within the neuronal cytoskeleton, J. Cell Biol. 98: 1523.PubMedCrossRefGoogle Scholar
  36. Hoffman, P. N., and Lasek, R. J., 1975, The slow component of axonal transport. Identification of major structural polypeptides of the axon and their generality among mammalian neurons, J. Cell Biol. 66: 351.PubMedCrossRefGoogle Scholar
  37. Hong, B., and Davison, P. F., 1981, Isolation and characterization of a soluble, immunoreactive peptide of glial fibrillary acidic protein, Biochim. Biophys. Acta 670: 139.PubMedGoogle Scholar
  38. Ip, W., Hartzer, M. K. Y-Y., Pang, S., and Robson, R. M., 1985, In vitro assembly of vimentin and its implications on the structure of intermediate filaments, J. Mol. Biol. 183: 365.PubMedCrossRefGoogle Scholar
  39. Jones, S. M., and Williams, C., 1982, Phosphate content of mammalian neurofilaments, J. Biol. Chem. 257: 9902.PubMedGoogle Scholar
  40. Julien, J. P., and Mushynski, W. E., 1982, Multiple phosphorylation sites in mammalian neurofilament polypeptides, J. Biol. Chem. 257: 10467.PubMedGoogle Scholar
  41. Julien, J. P., and Mushynski, W. E., 1983, The distribution of phosphorylation sites among identified proteolytic fragments of mammalian neurofilaments, J. Biol. Chem. 258: 4019.PubMedGoogle Scholar
  42. Kaufmann, E., Geisler, N., and Weber, K., 1984, SDS-Page strongly overestimates the molecular masses of the neurofilament proteins, FEBS Lett. 170: 81.PubMedCrossRefGoogle Scholar
  43. Kaufmann, E., Weber, K., and Geisler, N., 1985, Intermediate filament forming ability of desmin derivatives lacking either the aminoterminal 67 or carboxyterminal 27 residues, J. Mol. Biol. 185: 733.PubMedCrossRefGoogle Scholar
  44. Lasek, R. J., Oblinger, M. M., and Drake, P. F., 1983, Molecular biology of neuronal geometry: Expression of neurofilament genes influences axonal diameter, Cold Spring Harbor Symp. Quant. Biol. 48: 731.PubMedGoogle Scholar
  45. Lazarides, E., 1982, Intermediate filaments: a chemically heterogenous developmentally regulated class of proteins, Ann. Rev. Biochem. 51: 219.PubMedCrossRefGoogle Scholar
  46. Lee, L. D., and Baden, H. P., 1976, Organization of the polypeptide chains in mammalian keratin, Nature 264:377.,PubMedCrossRefGoogle Scholar
  47. Lewis, A. S., and Cowan, N. J., 1985, Genetics, evolution and expression of the 68 Kd neurofilament protein: isolation of a cloned cDNA probe, J. Cell Biol. 100: 843.PubMedCrossRefGoogle Scholar
  48. Lewis, S. A., Balcarek, J. M., Krek, V., Shelanski, M., and Cowan, N. J., 1984, Sequence of a cDNA clone encoding mouse glial fibrillary acidic protein: Structural conservation of intermediate filaments, Proc. Natl. Acad. Sci. USA 81: 2743.PubMedCrossRefGoogle Scholar
  49. Liem, R. K. H., and Hutchinson, S. B., 1982, Purification of individual components of the neurofilament triplet: filament assembly from the 70,000-dalton subunit, Biochemistry 21: 3221.PubMedCrossRefGoogle Scholar
  50. Liem, R. K. H., Chin, S. S. M., Moraru, E., and Wang, E., 1985, Monoclonal antibodies to epitopes on different regions of the 200,000 Dalton neurofilament protein, Exp. Cell Res. 156: 419.PubMedCrossRefGoogle Scholar
  51. Lu, Y., and Johnson, P., 1983, The TV-terminal domain of desmin is not involved in intermediate filament formation: evidence from thrombic digestion studies, Int. J. Biol. Macromol. 5: 347.CrossRefGoogle Scholar
  52. Marchuk, D., McCrohon, S., and Fuchs, E., 1984, Remarkable conservation of structure among intermediate filament genes, Cell 39: 491.PubMedCrossRefGoogle Scholar
  53. McLachlan, A. D., 1978, Coiled coil formation and sequence regularities in the helical regions of a-keratin, J. Mol Biol. 124: 297.PubMedCrossRefGoogle Scholar
  54. McLachlan, A. D., and Karn J., 1982, Periodic charge distributions in the myosin rod amino acid sequence match cross-bridge spacings in muscle, Nature 299: 226.PubMedCrossRefGoogle Scholar
  55. McLachlan, A. D., and Stewart, M., 1975, Tropomyosin coiled-coil interactions: Evidence for an u McLachlan, A. D., and Stewart, M., 1976, The 14-fold periodicity in a-tropomyosin and the interaction with actin, J. Mol. Biol. 103: 271.CrossRefGoogle Scholar
  56. McLachlan, A. D., and Stewart, M., 1982, Periodic charge distribution in the intermediate filament proteins desmin and vimentin, J. Mol. Biol. 162: 693.PubMedCrossRefGoogle Scholar
  57. Milam, L., and Erickson, H. P., 1982, Visualization of a 21-nm axial periodicity in shadowed keratin filaments and neurofilaments, J. Cell Biol. 94: 592.PubMedCrossRefGoogle Scholar
  58. Milstone, L. M., 1981, Isolation and characterization of two polypeptides that form intermediate filaments in bovine esophageal epithelium, J. Cell Biol. 88: 317.PubMedCrossRefGoogle Scholar
  59. Moll, R., Franke, W. W., Schiller, D., Geiger, B., and Krepler, R., 1982, The catalog of human cytokeratins: Patterns of expression in normal epithelia, tumors, and cultured cells, Cell 31: 11.PubMedCrossRefGoogle Scholar
  60. Nelson, W. J., and Traub, P., 1981, Properties of a Ca2 + -activated protease specific for the intermediate-sized filament protein vimentin in Ehrlich ascitis tumour cells, Eur. J. Biochem. 116: 51.PubMedCrossRefGoogle Scholar
  61. Nelson, W. J., and Traub, P., 1983, Proteolysis of vimentin and desmin by the Ca2 +-activated proteinase specific for these intermediate filament proteins, Mol. Cell Biol. 3: 1146.PubMedGoogle Scholar
  62. Nelson, W. J., Vorgias, C. E., and Traub, P., 1982, A rapid method for the large scale purification of the intermediate filament protein vimentin by single-stranded DNA-cellulose affinity chromatography, Biochem. Biophys. Res. Commun. 106: 1145.CrossRefGoogle Scholar
  63. Osborn, M., Geisler, N., Shaw, G., Sharp, G., and Weber, K., 1982, Intermediate filaments, Cold Spring Harbor Symp. Quant. Biol. 46: 413.PubMedGoogle Scholar
  64. Pang, Y. Y-S., Robson, R. M., Hartzer, M. K., and Stromer, M. H., 1983, Subunit structure of the desmin and vimentin protofilament units, J. Cell Biol. 97: 226a.Google Scholar
  65. Parry, D. A. D., 1981, Structure of rabbit skeletal muscle. Analysis of the amino acid sequences of two fragments from the rod region, J. Mol. Biol. 153: 459.PubMedCrossRefGoogle Scholar
  66. Parry, D. A. D., Crewther, W. G., Fraser, R. D. B., and McRae, T. P., 1977, Structure of cx-keratin: structural implication of the amino acid sequences of the type I and type II chain segments, J. Mol. Biol. 113: 449.PubMedCrossRefGoogle Scholar
  67. Pruss, R. M., Mirsky, R., Raff, M. C., Thorpe, R., Dowding, A. J., and Anderton, B. H., 1981, Cell classes of intermediate filaments share a common antigenic determinant defined by a monoclonal antibody, Cell 37: 419.CrossRefGoogle Scholar
  68. Quax, W. J., Egberts, W. V., Hendriks, W., Quax-Jeuken, Y., and Bloemendal, H., 1983, The structure of the vimentin gene, Cell 35: 215.PubMedCrossRefGoogle Scholar
  69. Quax, W., Van Den Heuvel, R., Egberts, W. V., Quax-Jeuken, Y., and Bloemendal, H., 1984, Intermediate filament cDNAs from BHK-21 cells: Demonstration of distinct genes for desmin and vimentin in all vertebrate classes, Proc. Natl. Acad. Sci. USA 81: 5970.PubMedCrossRefGoogle Scholar
  70. Quinlan, R. A., and Franke, W. W., 1982, Heteropolymer filaments of vimentin and desmin in vascular smooth muscle tissue and cultured hamster kidney cells demonstrated by chemical crosslinking, Proc. Natl. Acad. Sci. USA 79: 3452.PubMedCrossRefGoogle Scholar
  71. Quinlan, R. A., and Franke, W. W., 1983, Molecular interactions in intermediate-sized filaments revealed by chemical crosslinking, Eur. J. Biochem. 132: 477.PubMedCrossRefGoogle Scholar
  72. Quinlan, R. A., Cohlberg, J. A., Schiller, D. L., Hatzfeld, M., and Franke, W. W., 1984, Heterotypic tetramer (A2D2) complex of non-epidermal keratins isolated from the cytoskeletons of rat hepatocytes and hepatoma cells, J. Mol. Biol. 178: 365.PubMedCrossRefGoogle Scholar
  73. Renner, W., Franke, W. W., Schmid, E., Geisler, N., Weber, K., and Mandelkow, E., 1981, Reconstitution of intermediate-sized filaments from denatured monomeric vimentin, J. Mol. Biol. 149: 285.PubMedCrossRefGoogle Scholar
  74. Rueger, D-C., Huston, J. S., Dahl, D., and Bignami, A., 1979, Formation of 100 Å filaments from purified glial fibrillary acidic protein in vitro, J. Mol. Biol. 137: 53.CrossRefGoogle Scholar
  75. Sharp, G., Shaw, G., and Weber, K., 1982, Immunoelectronmicroscopical localization of the three neurofilament triplet proteins along neurofilaments of cultured dorsal root ganglion neurones, Exp. Cell Res. 137: 403.PubMedCrossRefGoogle Scholar
  76. Skerrow, D., Matoltsy, A. G., and Matoltsy, M. N., 1973, Isolation and characterization of the α- helical regions of epidermal prekeratin,J. Biol. Chem. 248:4820.Google Scholar
  77. Sodek, J., Hodges, R. S., Smillie, L. B., and Jurasek, L., 1972, Amino-acid sequence of rabbit skeletal tropomyosin and its coiled-coil structure, Proc. Natl. Acad. Sci. USA 69: 3800.PubMedCrossRefGoogle Scholar
  78. Sparrow, L. G., and Inglis, A. S., 1980, Characterization of the cyanogen bromide peptides of component 7c, a major microfibrillar protein from wool in: Proceedings of the 6th Quinquennial International Wool Textile Research Conference, Pretoria, Vol. 2, pp. 237 –246.Google Scholar
  79. Steinert, P. M., 1978, Structure of the three-chain unit of the bovine epidermal keratin filament, J. Mol. Biol. 123: 49.PubMedCrossRefGoogle Scholar
  80. Steinert, P. M., Idler, W. W., and Zimmermann, S. B., 1976, Self-assembly of bovine epidermal keratin filaments in vitro, J. Mol. Biol. 108: 547.PubMedCrossRefGoogle Scholar
  81. Steinert, P. M., Zimmermann, S. B., Starger, J. M., and Goldman, R. D., 1978, Ten-nanometer filaments of hamster BHK-21 cells and epidermal keratin filaments have similar structures, Proc. Natl. Acad. Sci. USA 75: 6098.PubMedCrossRefGoogle Scholar
  82. Steinert, P. M., Idler, W. W., and Goldman, R. D., 1980, Intermediate filaments of baby hamster kidney (BHK-21) cells and bovine epidermal keratinocytes have similar ultrastructures and subunit structures, Proc. Natl. Acad. Sci. USA 77: 4534.PubMedCrossRefGoogle Scholar
  83. Steinert, P. M., Idler, W. W., Cabral, F., Gottesman, M. M., and Goldman, R. D., 1981, In vitro assembly of homopolymer and copolymer filaments from intermediate filament subunits of muscle and fibroblastic cells, Proc. Natl. Acad. Sci. USA 78: 3692.PubMedCrossRefGoogle Scholar
  84. Steinert, P. M., Rice, R. H., Roop, D. R., Trus, B. L., and Steven, A. C., 1983, Complete amino acid sequence of a mouse epidermal keratin subunit and implications for the structure of intermediate filaments, Nature 302: 794.PubMedCrossRefGoogle Scholar
  85. Steinert, P. M., Parry, D. A. D., Racoosin, E. L., Joller, W. W., Steven, A. C., Trus, B. L., and Roop, D. R., 1984, The complete cDNA and deduced amino acid sequences of a type II mouse epidermal keratin of 60,000 Da: Analysis of the sequence differences between type I and type II keratins, Proc. Natl. Acad. Sci. USA 81: 5709.PubMedCrossRefGoogle Scholar
  86. Steven, A. C., Wall, J., Hainfield, J. F., and Steinert, P. M., 1982, Structure of fibroblastic intermediate filaments: analysis by scanning transmission electron microscopy, Proc. Natl. Acad. Sci. USA 79: 3101.PubMedCrossRefGoogle Scholar
  87. Steven, A. C., Hainfield, J. F., Trus, B. L., Wall, J. S., and Steinert, P. M., 1983, The distribution of mass in heteropolymer intermediate filaments assembled in vitro, J. Cell Biol. 97: 1939.PubMedCrossRefGoogle Scholar
  88. Stromer, M. H., Huiatt, T. W., Richardson, F. L., and Robson, R. M., 1981, Disassembly of synthetic 10-nm filaments from smooth muscle into protofilaments, Eur. J. Cell Biol. 25: 136.PubMedGoogle Scholar
  89. Traub, P., and Vorgias, C. E., 1983, Involvement of the N-terminal polypeptide of vimentin in the formation of intermediate filaments, J. Cell Sci. 63: 43.PubMedGoogle Scholar
  90. Traub, P., and Vorgias, C. E., 1984, Differential effect of arginine modification with 1,2- cyclohexanedione on the capacity of vimentin and desmin to assemble into intermediate filaments and to bind to nucleic acids, J. Cell Sci. 65: 1.PubMedGoogle Scholar
  91. Weber, K., and Geisler, N., 1982, The structural relation between intermediate filament proteins in living cells and the a-keratins of sheep wool, EMBO J. 1: 1155.PubMedGoogle Scholar
  92. Weber, K., and Geisler, N., 1983, Proteolysis of the neurofilament 68 kDa protein explains several previously described brain proteins of unique composition and high acidity, FEBS Lett. 164: 129.PubMedCrossRefGoogle Scholar
  93. Weber, K., and Geisler, N., 1984, Intermediate filaments—From wool a-keratins to neurofilaments: a structural overview, in: Cancer Cells, Vol. 1, The Transformed Phenotype, pp. 153–159, Cold Spring Harbor Laboratory, Cold Spring Harbor, NY.Google Scholar
  94. Willard, M. B., and Simon, C., 1981, Antibody decoration of neurofilaments, J. Cell Biol. 89: 198.PubMedCrossRefGoogle Scholar
  95. Woods, E. F., and Gruen, L. C., 1981, Structural studies on the microfibrillar proteins of wool: characterization of the a-helix-rich particle produced by chymotryptic digestion, Austr. J. Biol. Sci. 34: 515Google Scholar

Copyright information

© Plenum Press, New York 1986

Authors and Affiliations

  • Norbert Geisler
    • 1
  • Klaus Weber
    • 1
  1. 1.Max Planck Institute for Biophysical ChemistryGoettingenFederal Republic of Germany

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