Hostname: page-component-cd9895bd7-7cvxr Total loading time: 0 Render date: 2024-12-27T09:24:00.540Z Has data issue: false hasContentIssue false
  • English
  • Français

Neutron Scattering in Structural Biology and Biomolecular Materials

Published online by Cambridge University Press:  29 November 2013

J. Kent Blasie  and
Peter Timmins
Get access

Extract

The substantial power of both elastic and inelastic neutron-scattering techniques for the investigation of the structure and dynamics of biological systems and related biomolecular-based materials—as with soft matter in the previous article by Lindner and Wignall—arises primarily from the essentially isomorphous nature of the substitution of deuterium for selected hydrogen atoms in these systems, coupled with the exquisite sensitivity of neutron scattering to this isotopic substitution. Since these systems are comprised of large macromolecules and supramolecular assemblies thereof, their essential structures and dynamics extend from the atomic scale up to very large length scales of the Order of 101–104 Å. Hence neutron sources and neutron-scattering spectrometers optimized for longer wavelength (or “cold”) thermal neutrons are necessary in order to most effectively address the structure and dynamics at the longer length scales inherent to these Systems.

The large majority of previous neutron-scattering experiments on biological systems have been performed with reactor neutron sources. Some of the more significant of these are briefly summarized in the following sections. They may be categorized in terms of the nature of the intermolecular order, both orientational and positional, within the System of interest and either the elastic neutron-scattering technique employed to investigate their time-averaged structures or the inelastic neutron-scattering technique employed to investigate their dynamics.

Type
Neutron Scattering in Materials Research
Information
MRS Bulletin , Volume 24 , Issue 12 , December 1999 , pp. 40 - 47
Copyright
Copyright © Materials Research Society 1999

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)

References

1.Capel, M.S., Kjeldgaard, M., Engelman, D.M., and Moore, P.B., J. Mol. Biol. 200 (1988) p. 65.CrossRefGoogle Scholar
2.Olah, G.A. and Trewhella, J., Biochemistry 33 (1994) p. 12800.CrossRefGoogle Scholar
3.Mendelson, R.A., Timmins, P.A., Schneider, D.K., Krylova, I., Ramos, C.H.I., Reinach, F.C., and Stone, D.B., J. Mol. Biol. 281 (1998) p. 689.Google Scholar
4.Schaftheutle, M.E., Setlikova, E., Timmins, P.A., Johner, H., Gutgesell, P., Setlik, I., and Welte, W., Biochemistry 29 (1990) p. 1216.CrossRefGoogle Scholar
5.Hunt, J.F., McCrea, D., Zaccai, G., and Engelman, D.M., J. Mol. Biol. 273 (1997) p. 1004.CrossRefGoogle Scholar
6.Büldt, G., Gally, U., Seelig, J., and Zaccai, G., J. Mol. Biol. 134 (1979) p. 673.CrossRefGoogle Scholar
7.Zaccai, G., Büldt, G., Seelig, A., and Seelig, J., J. Mol. Biol. 134 (1979) p. 693.CrossRefGoogle Scholar
8.Tu, K., Tobias, D.J., and Klein, M.L., Biophys. J. 69 (1995) p. 2558.CrossRefGoogle Scholar
9.Tu, K., Tobias, D.J., Blasie, J.K., and Klein, M.L., Biophys. J. 70 (1996) p. 595.CrossRefGoogle Scholar
10.Herbette, L., DeFoor, P., Fleischer, S., Pascolini, D., Scarpa, A., and Blasie, J.K., Biochim. Biophys. Acta 817 (1985) p. 103.CrossRefGoogle Scholar
11.Pachence, J.M., Dutton, P.L., and Blasie, J.K., Biochim. Biophys. Acta Bioenerg. 635 (1981) p. 267.CrossRefGoogle Scholar
12.Pachence, J.M., Dutton, P.L., and Blasie, J.K., Biochim. Biophys. Acta 724 (1983) p. 6.CrossRefGoogle Scholar
13.Engelman, D.M. and Zaccai, G., Proc. Natl. Acad. Sci. U.S.A. 77 (1980) p. 5894.CrossRefGoogle Scholar
14.Fuller, W., Forsyth, V.T., Mahendrasingam, A., Langan, P., Pigram, W.J., Mason, S.A., and Wilson, C.C., in Neutrons in Biology, edited by Schoenborn, B.P. and Knott, R.B. (Plenum Press, New York, 1996) p. 345.CrossRefGoogle Scholar
15.Nambudripad, R., Stark, W., Opella, S.J., and Makowski, L., Science 252 (1991) p. 1221.CrossRefGoogle Scholar
16.Cheng, X. and Schoenborn, B.P., Acta Crystallogr., Sect. B 46 (1990) p. 195.CrossRefGoogle Scholar
17.Shu, F., Schoenborn, B.P., and Ratnakrishnan, V., “The Neutron Structure of a Fully Deuterated Protein: Direct Detection of Hydrogen Bonds and Histidine Protonation States in Myoglobin,” Proc. Natl. Acad. Sci. U.S.A., submitted for publication, 1999.Google Scholar
18.Pebay-Peyroula, E., Garavito, R.M., Rosenbusch, J.P., Zulauf, M., and Timmins, P.A., Structure 3 (1995) p. 1051.CrossRefGoogle ScholarPubMed
19.Doster, W., Cusack, S., and Petry, W., Nature 337 (1989) p. 754.CrossRefGoogle Scholar
20.Ferrand, M., Dianoux, A.J., Petry, W., and Zaccai, G., Proc. Natl. Acad. Sci. U.S.A. 90 (1993) p. 9668.CrossRefGoogle Scholar
21.Cusack, S., Büttner, H., Ferrand, M., Langan, P., and Timmins, P., eds., Biological Macromolecular Dynamics (Adenine Press, New York, 1997).Google Scholar
22.Robertson, D.E., Farid, R.S., Moser, C.C., Urbauer, J.L., Mulholland, S.E., Pidikiti, R., Lear, J.D., Wand, A.J., DeGrado, W.F., and Dutton, P.L., Nature 368 (1994) p. 425.CrossRefGoogle Scholar
23.Choma, C.T., Lear, J.D., Nelson, M.J., Dutton, P.L., Robertson, D.E., and DeGrado, W.F., J. Am. Chem. Soc. 116 (1994) p. 856.CrossRefGoogle Scholar
24.Strzalka, J., Chen, X., Dutton, P.L., Ocko, B.M., and Blasie, J.K., “Structural Studies of Model Metalloprotein Maquettes Vectorially Oriented at a Soft Interface: Langmuir Monoayers,” Langmuir, submitted for publication, 1999.Google Scholar
25.Strzalka, J., Chen, X., Dutton, P.L., and Blasie, J.K., “Structural Studies of Model Metalloprotein Maquettes Vectorially Oriented at a Soft Interface: Langmuir-Blodgett Monolayers,” Langmuir, submitted for publication, 1999.Google Scholar
26.Kneller, L.R., Edwards, A.M., Majkrzak, C.F., Berk, N.F., Krueger, S., and Blasie, J.K., “Hydration State of a Single Cytochromec Monolayer Vectorially Oriented at a Soft Interface Investigated via Neutron Interferometry,” Biophys. J., submitted for publication, 1999.Google Scholar
27.Pilloud, D.L., Farid, R.S., Rabanal, F., Gibney, B.R., Dutton, P.L., and Moser, C.C., J. Phys. Chem. B 102 (1998) p. 1926.CrossRefGoogle Scholar
28.Niimura, N., Minezaki, Y., Nonaka, T., Castagna, J.C., Cipriani, F., Hoghoj, P., Lehmann, M.S., and Wilkinson, C., Nat. Struct. Biol. 4 (1997) p. 909.CrossRefGoogle Scholar
29.Strzalka, J., Chen, X., Gibney, B.R., Moser, C.C., Dutton, P.L., Ocko, B.M., Satija, S., and Blasie, J.K., “X-ray and Neutron Reflectivity Studies of Mixed Langmuir Monolayers of a Lipopeptide Maquette and a Phospholipid” (unpublished manuscript).Google Scholar