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MeSH Review

Neutron Diffraction

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Disease relevance of Neutron Diffraction


High impact information on Neutron Diffraction


Biological context of Neutron Diffraction


Associations of Neutron Diffraction with chemical compounds

  • Neutron diffraction maps have been used to assign the rotor conformations of the hydroxyl hydrogens in trypsin [9].
  • Low-angle neutron diffraction patterns from oriented fibrin made in the presence of EDTA, made in the presence of calcium, or stabilized with factor XIIIa are very similar, showing that the packing of the molecules within the fibers is the same or very similar in these different preparations [10].
  • The calculated head-group spacings at minimum hydration are consistent with those obtained from neutron diffraction and indicate that the methyl groups of the choline are almost in contact with corresponding groups in the opposing bilayer [11].
  • The result confirms the stereochemistry of the malate/succinate transformation, as well as the NAD+/NADH interconversion, and demonstrates the usefulness of the single-crystal neutron diffraction method for determining the absolute configuration of molecules having a chiral monodeuteriomethylene group [12].
  • Orientation of histidine residues in RNase A: neutron diffraction study [13].

Gene context of Neutron Diffraction


Analytical, diagnostic and therapeutic context of Neutron Diffraction


  1. Crystallization and preliminary neutron analysis of the dissimilatory sulfite reductase D (DsrD) protein from the sulfate-reducing bacterium Desulfovibrio vulgaris. Chatake, T., Mizuno, N., Voordouw, G., Higuchi, Y., Arai, S., Tanaka, I., Niimura, N. Acta Crystallogr. D Biol. Crystallogr. (2003) [Pubmed]
  2. Crystals of trp repressor suitable for high-resolution neutron Laue diffraction studies. Daniels, B.V., Myles, D.A., Forsyth, V.T., Lawson, C.L. Acta Crystallogr. D Biol. Crystallogr. (2003) [Pubmed]
  3. Effect of protein packing structure on side-chain methyl rotor conformations. Kossiakoff, A.A., Shteyn, S. Nature (1984) [Pubmed]
  4. First solvation shell of the Cu(II) aqua ion: evidence for fivefold coordination. Pasquarello, A., Petri, I., Salmon, P.S., Parisel, O., Car, R., Toth, E., Powell, D.H., Fischer, H.E., Helm, L., Merbach, A. Science (2001) [Pubmed]
  5. Neutron diffraction analysis of myoglobin: structure of the carbon monoxide derivative. Norvell, J.C., Nunes, A.C., Schoenborn, B.P. Science (1975) [Pubmed]
  6. The hydration structure of guanidinium and thiocyanate ions: implications for protein stability in aqueous solution. Mason, P.E., Neilson, G.W., Dempsey, C.E., Barnes, A.C., Cruickshank, J.M. Proc. Natl. Acad. Sci. U.S.A. (2003) [Pubmed]
  7. The crystal and molecular structure of the antifolate drug trimethoprim (2,4-diamino-5-(3,4,5-trimethoxybenzyl)pyrimidine). A neutron diffraction study. Koetzle, T.F., Williams, G.J. J. Am. Chem. Soc. (1976) [Pubmed]
  8. The in vitro binding of acetaldehyde to collagen studied by neutron diffraction. Wess, T.J., Wess, L., Miller, A. Alcohol Alcohol. (1994) [Pubmed]
  9. Hydroxyl hydrogen conformations in trypsin determined by the neutron diffraction solvent difference map method: relative importance of steric and electrostatic factors in defining hydrogen-bonding geometries. Kossiakoff, A.A., Shpungin, J., Sintchak, M.D. Proc. Natl. Acad. Sci. U.S.A. (1990) [Pubmed]
  10. Fibrinogen and fibrin structure and fibrin formation measured by using magnetic orientation. Freyssinet, J.M., Torbet, J., Hudry-Clergeon, G., Maret, G. Proc. Natl. Acad. Sci. U.S.A. (1983) [Pubmed]
  11. The partial molar volume of water in biological membranes. Scherer, J.R. Proc. Natl. Acad. Sci. U.S.A. (1987) [Pubmed]
  12. Determination of the absolute configuration of (-)-(2R)-succinic-2-d acid by neutron diffraction study: unambiguous proof of the absolute stereochemistry of the NAD+/NADH interconversion. Yuan, H.S., Stevens, R.C., Fujita, S., Watkins, M.I., Koetzle, T.F., Bau, R. Proc. Natl. Acad. Sci. U.S.A. (1988) [Pubmed]
  13. Orientation of histidine residues in RNase A: neutron diffraction study. Wlodawer, A., Sjölin, L. Proc. Natl. Acad. Sci. U.S.A. (1981) [Pubmed]
  14. Membrane-bound ARF1 peptide: interpretation of neutron diffraction data by molecular dynamics simulation methods. Balali-Mood, K., Harroun, T.A., Bradshaw, J.P. Mol. Membr. Biol. (2005) [Pubmed]
  15. Beta-amyloid 25 to 35 is intercalated in anionic and zwitterionic lipid membranes to different extents. Dante, S., Hauss, T., Dencher, N.A. Biophys. J. (2002) [Pubmed]
  16. Neutron diffraction reveals sequence-specific membrane insertion of pre-fibrillar islet amyloid polypeptide and inhibition by rifampicin. Balali-Mood, K., Ashley, R.H., Hauss, T., Bradshaw, J.P. FEBS Lett. (2005) [Pubmed]
  17. Molecular dynamics study of polarizable ion models for molten AgBr. Bitrian, V., Trullàs, J. The journal of physical chemistry. B, Condensed matter, materials, surfaces, interfaces & biophysical. (2006) [Pubmed]
  18. Hydrogen exchange in RNase A: neutron diffraction study. Wlodawer, A., Sjölin, L. Proc. Natl. Acad. Sci. U.S.A. (1982) [Pubmed]
  19. Magnetism and structural chemistry of the n = 1 Ruddlesden-Popper phases La4LiMnO8 and La3SrLiMnO8. Burley, J.C., Battle, P.D., Gallon, D.J., Sloan, J., Grey, C.P., Rosseinsky, M.J. J. Am. Chem. Soc. (2002) [Pubmed]
  20. A structural study of the myristoylated N-terminus of ARF1. Harroun, T.A., Bradshaw, J.P., Balali-Mood, K., Katsaras, J. Biochim. Biophys. Acta (2005) [Pubmed]
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