Disease relevance of Neutron Diffraction

• Dissimilatory sulfite reductase D (DsrD) from Desulfovibrio vulgaris has been crystallized for a neutron diffraction study [1].
• Crystallization and preliminary neutron-diffraction measurements of wild-type variant Val58-->Ile of the Escherichia coli trp repressor are reported [2].

High impact information on Neutron Diffraction

• We report here an investigation of the rotational conformations of the methyl groups of aliphatic side chains in the protein crambin by neutron diffraction [3].
• We determined the structure of the hydrated Cu(II) complex by both neutron diffraction and first-principles molecular dynamics [4].
• Neutron diffraction analysis of myoglobin: structure of the carbon monoxide derivative [5].
• The locations of hydrogen and deuterium atoms and water molecules have been investigated in carbon monoxide myoglobin using neutron diffraction, and the results are compared with earlier work on metmyoglobin [5].
• Neutron diffraction experiments were carried out on aqueous solutions containing either guanidinium or thiocyanate ions [6].

Biological context of Neutron Diffraction

• The crystal and molecular structure of the antifolate drug trimethoprim (2,4-diamino-5-(3,4,5-trimethoxybenzyl)pyrimidine). A neutron diffraction study [7].
• The location of acetaldehyde binding sites in the axial unit cell of tendon collagen was investigated by neutron diffraction [8].

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

• Membrane-bound ARF1 peptide: interpretation of neutron diffraction data by molecular dynamics simulation methods [14].
• Neutron diffraction with the use of selectively deuterated amino acids has allowed us to determine unambiguously the position of the neurotoxic fragment Abeta (25-35) in the membrane [15].
• In the first structural study of membrane-associated hIAPP, lamellar neutron diffraction shows that oligomeric hIAPP inserts into phospholipid bilayers, and extends across the membrane [16].
• The PIM1 reproduces the broad main peak of the total structure factor present in the neutron diffraction data, although the smoothed three-peak feature of this broad peak is slightly overestimated [17].
• Hydrogen exchange in RNase A: neutron diffraction study [18].

Analytical, diagnostic and therapeutic context of Neutron Diffraction

• Polycrystalline samples of La4LiMnO8 and La3SrLiMnO8 have been studied by a combination of X-ray diffraction (XRD), neutron diffraction (ND), 6Li MAS NMR, electron microscopy (EM), and magnetometry [19].
• The effect of myristoylation on the 15-amino-acid peptide from the membrane-binding N-terminus of ADP ribosylation factor 1 (ARF1) was studied using neutron diffraction and circular dichroism [20].

References