title: Preliminary neutron crystallographic study of human transthyretin.
abstract: Preliminary studies of perdeuterated crystals of human transthyretin (TTR) have been carried out using the LADI-III and D19 diffractometers at the Institut Laue-Langevin in Grenoble. The results demonstrate the feasibility of a full crystallographic analysis to a resolution of 2.0 Å using Laue diffraction and also illustrate the potential of using monochromatic instruments such as D19 for higher resolution studies where larger crystals having smaller unit cells are available. This study will yield important information on hydrogen bonding, amino-acid protonation states and hydration in the protein. Such information will be of general interest for an understanding of the factors that stabilize/destabilize TTR and for the design of ligands that may be used to counter TTR amyloid fibrillogenesis.
authors.affiliation: EPSAM, Keele University, Keele, Staffordshire ST5 5BG, England.
authors.forename: Melina
authors.initials: M
authors.lastname: Haupt
authors.forename: Matthew P
authors.initials: MP
authors.lastname: Blakeley
authors.forename: Susana C M
authors.initials: SC
authors.lastname: Teixeira
authors.forename: Sax A
authors.initials: SA
authors.lastname: Mason
authors.forename: Edward P
authors.initials: EP
authors.lastname: Mitchell
authors.forename: Jonathan B
authors.initials: JB
authors.lastname: Cooper
authors.forename: V Trevor
authors.initials: VT
authors.lastname: Forsyth
mesh_terms: D006801:Humans; D006860:Hydrogen Bonding; D033363:Neutron Diffraction; D011228:Prealbumin / Q000737:chemistry*; D014867:Water / Q000737:chemistry
chemical_list: D011228:Prealbumin; D014867:Water
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