Preliminary neutron crystallographic study of human transthyretin | Zendy

Haupt Melina | Zendy; Blakeley Matthew P. | Zendy; Teixeira Susana C. M. | Zendy; Mason Sax A. | Zendy; Mitchell Edward P. | Zendy; Cooper Jonathan B. | Zendy; Forsyth V. Trevor | Zendy

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Preliminary neutron crystallographic study of human transthyretin

Author(s) -

Haupt Melina,

Blakeley Matthew P.,

Teixeira Susana C. M.,

Mason Sax A.,

Mitchell Edward P.,

Cooper Jonathan B.,

Forsyth V. Trevor

Publication year - 2011

Publication title -

acta crystallographica section f

Language(s) - English

Resource type - Journals

ISSN - 1744-3091

DOI - 10.1107/s1744309111036244

Subject(s) - transthyretin , crystallography , protonation , neutron diffraction , resolution (logic) , materials science , neutron , hydrogen bond , chemistry , crystal structure , molecule , physics , computer science , organic chemistry , medicine , ion , quantum mechanics , artificial intelligence

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.

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