Ontology highlight
ABSTRACT:
SUBMITTER: Davies HA
PROVIDER: S-EPMC4788682 | biostudies-literature | 2016 Apr
REPOSITORIES: biostudies-literature
Biomolecular NMR assignments 20150916 1
Thirty-one proteins are known to form extracellular fibrillar amyloid in humans. Molecular information about many of these proteins in their monomeric, intermediate or fibrillar form and how they aggregate and interact to form the insoluble fibrils is sparse. This is because amyloid proteins are notoriously difficult to study in their soluble forms, due to their inherent propensity to aggregate. Using recent developments in fast NMR techniques, band-selective excitation short transient and band- ...[more]