Applications of Neutron Scattering to Biology
DOI: 10.1063/1.881011
During the past 20 years neutron scattering has developed into an important tool for the determination of the structure of biologically important compounds. Traditionally these kinds of problems have been solved by x‐ray crystallography or electron microscopy, both of which require far cheaper and simpler instrumentation. The justification for the use of neutrons in biological research, which might seem at first an outrageous extravagance, is contained in a single word: “hydrogen.” The scattering of neutrons from hydrogen (and deuterium) is far larger compared to other atoms than is the comparative scattering of x rays and electrons; neutrons, therefore, are a much better probe for these light atoms.
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References
1. G. E. Schulz, R. H. Schirmer, Principles of Protein Structure, Springer‐Verlag, New York (1979).
2. G. E. Bacon, Neutron Diffraction, Third Edition, Oxford U.P., London (1975).
3. A. Wlodawer, L. Sjölin, Proc. Nat. Acad. Sci. USA 79, 1418 (1982).https://doi.org/PNASA6
4. C. K. Woodward, B. D. Hilton, Ann. Rev. Biophys. Bioengin. 8, 99 (1979).
5. J. Rosa, F. M. Richards, J. Mol. Biol. 145, 835 (1981).https://doi.org/JMOBAK
6. G. Wagner, K. Wüthrich, J. Mol. Biol. 120, 31 (1979).https://doi.org/JMOBAK
7. J. C. Norvell, B. P. Schoenborn, “The Structure of Carbon Monoxide Myoglobin: Real Space Refinement,” Brookhaven Symposia in Biology 27, Brookhaven National Laboratory, Upton, N.Y. (BNL 560453), p. 11 (1976).
8. B. P. Schoenborn, ed., Neutrons in Biology. Proc. of the 32nd Brookhaven Symposia in Biology. Plenum, New York (1984).
9. H. B. Stuhrmann, “Contrast Variation,” in Small Angle X‐ray Scattering, O. Glatter, O. Kratky, eds., Academic, London (1982).
10. J. F. Pardon, D. L. Worcester, J. C. Wooley, P. I. Cotter, D. M. J. Lilley, D. M. Richards, Nucleic Acids Res. 4, 3199 (1977).https://doi.org/NARHAD
11. P. Suau, G. G. Kneale, G. W. Braddock, J. P. Baldwin, E. M. Bradbury, Nucleic Acids Res. 4, 3769 (1977).https://doi.org/NARHAD
12. A. Klug, “Nucleosome Chromatin Superstructure,” in Nucleic Acid Research, K. Mizobucki, I. Watanabe, J. D. Watson, eds., Academic, Tokyo (1983).
13. M. G. Rossman, C. Abad‐Sapatero, M. A. Hermodson, J. W. Erickson, J. Mol. Biol. 166, 37 (1983).https://doi.org/JMOBAK
14. S. Cusack, “Neutron Scattering Studies of Virus Structure,” in Neutrons in Biology. Proc. of the 32nd Brookhaven Symposia in Biology, B. P. Schoenborn, ed., Plenum, New York (1984).
15. Z. Q. Li, R. Giege, B. Jacrot, R. Oberthür, J.‐C. Thierry, G. Zaccai, Biochemistry 22, 4380 (1983).https://doi.org/BICHAW
16. G. Büldt, “Specific Deuteration and Membrane Structure,” in Neutrons in Biology. Proc. of the 32nd Brookhaven Symposia in Biology, B. P. Schoenborn, ed., Plenum, New York, (1984).
17. P. Stoeckel, R. May, I. Strell, Z. Geha, W. Hoppe, H. Heumann, W. Zillig, H. L. Crespi, J. Appl. Crystallogr. 12, 176 (1979).https://doi.org/JACGAR
18. V. R. Ramakrishnan, M. Capel, M. Kjeldgaard, D. M. Engelman, P. B. Moore, J. Mol. Biol. 174, 265 (1984); https://doi.org/JMOBAK
M. Capel, M. Kjeldgaard, D. M. Engelman, P. B. Moore, unpublished data.19. K. H. Nierhaus, R. Lietzke, R. P. May, V. Nowotny, H. Schulze, K. Simpson, P. Wurrnbach, H. B. Stuhrmann, Proc. Natl. Acad. Sci. USA 80, 2889 (1983).https://doi.org/PNASA6
20. D. M. Engelman, A. J. Dianoux, S. Cusack, B. Jacrot, “Inelastic Neutron Scattering Studies of Hexokinase,” Neutrons in Biology. Proc. of the 32nd Brookhaven Symposia in Biology, B. P. Schoenborn, ed., Plenum, New York (1984).
21. H. D. Middendorf, J. T. Randall, H. L. Crespi, “Neutron Spectroscopy of Hydrogenous and Biosynthetically Deuterated Proteins,” Neutrons in Biology. Proc. of the 32nd Brookhaven Symposia in Biology, B. P. Schoenborn, ed., Plenum, New York (1984).
22. G. Stoeffler, M. Stoeffler‐Meilicke, Am. Rev. Biophys. Bioengineer 13, 303 (1984).
More about the authors
Peter B. Moore, Yale University.
