Ontology highlight
ABSTRACT:
SUBMITTER: Haupt M
PROVIDER: S-EPMC4224461 | biostudies-literature | 2014 Nov
REPOSITORIES: biostudies-literature
Haupt Melina M Blakeley Matthew P MP Fisher Stuart J SJ Mason Sax A SA Cooper Jon B JB Mitchell Edward P EP Forsyth V Trevor VT
IUCrJ 20141021 Pt 6
Human transthyretin has an intrinsic tendency to form amyloid fibrils and is heavily implicated in senile systemic amyloidosis. Here, detailed neutron structural studies of perdeuterated transthyretin are described. The analyses, which fully exploit the enhanced visibility of isotopically replaced hydrogen atoms, yield new information on the stability of the protein and the possible mechanisms of amyloid formation. Residue Ser117 may play a pivotal role in that a single water molecule is closely ...[more]