Abstract
The term structure is used with different meanings in the biochemical literature. Sometimes it is used to describe the detailed atomic arrangement, as determined by X-ray diffraction; sometimes it is used for less detailed information. An example of the latter is topological information such as subunit A is close to subunit B, as may be deduced from, for example, cross-linking experiments.
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References
Amos, L. A., Henderson, R. and Unwin, P. N. T. (1982)Proc. Biophys. Mol Biol., 39, 183–231.
Brisson, A. and Wade, R. H. (1983)J. Mol Biol 166, 21–36.
Chang, J. J., Leonard, K., Arad, T., Pitt, T., Zhang, Y. X. and Zhang, L. H. (1982)J. Mol Biol., 161, 579–90.
Corless, J. M., McCaslin, D. R. and Scott, B. L. (1982)Proc. Natl. Acad. Sci. USA, 79, 1116–20.
Deatherage, J. F., Henderson, R. and Capaldi, R. A. (1982)J. Mol Biol., 158, 487–99.
Deatherage, J. F., Taylor, K. A. and Amos, L. A. (1983)J. Mol Biol. 167, 823–52.
Deisenhofer, J., Michel, H. and Huber, R. (1985)Trends Biochem. Sci., 10, 243–8.
Dorset, D. L., Engel, A., Haner, M., Massalski, A. and Rosenbusch, J. P. (1983)J. Mol Biol., 165, 701–10.
Fuller, S. D., Capaldi, R. A. and Henderson, R. (1979)J. Mol Biol., 134, 305–27.
Garavito, M., Jenkins, J., Jansonius, J. N., Karlsson, R. and Rosenbusch, J. P. (1983)J. Mol Biol., 164, 313–27.
Goldfarb, W., Frank, J., Kessel, M., Hsung,J. C., King, C. H. and King, T. E. (1979) in Cytochrome Oxidase (eds T. E. King et al.) Elsevier, Amsterdam, pp. 161–66.
Hebert, H., Jorgensen, P. L., Skriver, E. and Maunsbach, A. B. (1982)Biochim. Biophys Acta, 689, 571–4.
Henderson, R. and Shotton, D. (1980)J. Mol Biol., 139, 99–109.
Henderson, R. and Unwin, P. N. T. (1975)Nature (London), 257, 28–32.
Holser, W. T. (1958)Z. Kristallographie, 110, 266–81.
Hovmöller, S., Leonard, K. and Weiss, H. (1981)FEBS Lett., 123, 118–22.
Hovmöller, S., Slaughter, M., Berriman, J., Karlsson, B., Weiss, H. and Leonard, K. (1983) J. Mol Biol, 165, 401–6.
Hovmöller, S., Sjögren, A., Farrants, G., Sundberg, M. and Marinder, B.-O. (1984) Nature (London), 311, 238–1.
Jesior, J.-C. (1982)EMBO J., 1, 1423–8.
Karlsson, B., Hovmöller, S., Weiss, H. and Leonard, K. (1983)J. Mol Biol, 165, 287–302.
Karlsson, B., Vaara, T., Lounatmaa, K. and Gyllenberg, H. (1983)J. Bacteriol, 156, 1338–43.
Kistler, J., Stroud, R. M., Klymkowsky, M. W., Lalancette, R. A. and Fairclouch, R. H. (1982)Biophys. 37, 371–83.
Leifer, D. and Henderson, R. (1983) J. Mol Biol 163, 451–66.
Leonard, K., Wingfield, P., Arad, T. and Weiss, H. (1981)J. Mol Biol, 149, 259–74.
Mannella, C. (1982)J. Cell Biol, 94, 680–7.
Michel, H. (1982)J. Mol Biol, 158, 567–72.
Pearson, R. H. and Pascher, I. (1979)Nature (London), 281, 499–501.
Perkins, S. J. and Weiss, H. (1983)J. Mol Biol, 168, 847–66.
Sjögren, A., Hovmöller, S., Farrants, G., Ranta, H., Haapasalo, K., Ranta, K. and Lounatmaa, K. (1985)J. Bacteriol, 164, 1278–82.
Sleytr, U. B. and Messner, P. (1983)Annu. Rev. Microbiol, 37, 311–39.
Unwin, P. N. T. and Henderson, R. J. (1975)J. Mol Biol, 94, 425–40.
Unwin, P. N. T. and Zampighi, G. (1980)Nature (London), 283, 545–9.
Vanderkooi, G., Senior, A. E., Capaldi, R. A. and Hayashi, H. (1972)Biochim. Biophys. Acta, 274, 38–48.
Wingfield, P., Arad, T., Leonard, K. and Weiss, H. (1979)Nature (London), 280, 696–7.
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Hovmöller, S. (1986). Three-dimensional structure of membrane proteins. In: Ragan, C.I., Cherry, R.J. (eds) Techniques for the Analysis of Membrane Proteins. Springer, Dordrecht. https://doi.org/10.1007/978-94-009-4085-7_11
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DOI: https://doi.org/10.1007/978-94-009-4085-7_11
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