Ontology highlight
ABSTRACT:
SUBMITTER: De Simone A
PROVIDER: S-EPMC3344965 | biostudies-literature | 2012 May
REPOSITORIES: biostudies-literature
De Simone Alfonso A Kitchen Craig C Kwan Ann H AH Sunde Margaret M Dobson Christopher M CM Frenkel Daan D
Proceedings of the National Academy of Sciences of the United States of America 20120416 18
Protein molecules have evolved to adopt distinctive and well-defined functional and soluble states under physiological conditions. In some circumstances, however, proteins can self-assemble into fibrillar aggregates designated as amyloid fibrils. In vivo these processes are normally associated with severe pathological conditions but can sometimes have functional relevance. One such example is the hydrophobins, whose aggregation at air-water interfaces serves to create robust protein coats that h ...[more]