| Literature DB >> 18453706 |
Susana C M Teixeira1, Matthew P Blakeley, Ricardo M F Leal, Edward P Mitchell, V Trevor Forsyth.
Abstract
A preliminary neutron crystallographic study of the sweet protein thaumatin is presented. Large hydrogenated crystals were prepared in deuterated crystallization buffer using the gel-acupuncture method. Data were collected to a resolution of 2 A on the LADI-III diffractometer at the Institut Laue Langevin (ILL). The results demonstrate the feasibility of a full neutron crystallographic analysis of this structure aimed at providing relevant information on the location of H atoms, the distribution of charge on the protein surface and localized water in the structure. This information will be of interest for understanding the specificity of thaumatin-receptor interactions and will contribute to further understanding of the molecular mechanisms underlying the perception of taste.Entities:
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Year: 2008 PMID: 18453706 PMCID: PMC2376403 DOI: 10.1107/S1744309108008294
Source DB: PubMed Journal: Acta Crystallogr Sect F Struct Biol Cryst Commun ISSN: 1744-3091