Ontology highlight
ABSTRACT:
SUBMITTER: Ruggeri FS
PROVIDER: S-EPMC4525161 | biostudies-literature | 2015 Jul
REPOSITORIES: biostudies-literature
Ruggeri F S FS Longo G G Faggiano S S Lipiec E E Pastore A A Dietler G G
Nature communications 20150728
Amyloids are insoluble protein fibrillar aggregates. The importance of characterizing their aggregation has steadily increased because of their link to human diseases and material science applications. In particular, misfolding and aggregation of the Josephin domain of ataxin-3 is implicated in spinocerebellar ataxia-3. Infrared nanospectroscopy, simultaneously exploiting atomic force microscopy and infrared spectroscopy, can characterize at the nanoscale the conformational rearrangements of pro ...[more]