title: Designing supramolecular protein assemblies.
abstract: Many natural proteins self-assemble, either to fulfill their biological function or as part of a pathogenic process. Biological assembly phenomena such as amyloidogenesis, domain swapping and symmetric oligomerization are inspiring new strategies for designing proteins that self-assemble to form supramolecular complexes. Recent advances include the design of novel proteins that assemble into filaments, symmetric cages and regular arrays.
authors.affiliation: UCLA Department of Chemistry and Biochemistry, 611Charles E Young Drive East, University of California, Los Angeles, 90095-1569, USA. yeates@mbi@ucla.edu
authors.forename: Todd O
authors.initials: TO
authors.lastname: Yeates
authors.forename: Jennifer E
authors.initials: JE
authors.lastname: Padilla
mesh_terms: D000682:Amyloid / Q000737:chemistry; D046911:Macromolecular Substances; D008958:Models, Molecular; D036103:Nanotechnology; D011487:Protein Conformation; D015202:Protein Engineering / Q000379:methods* / Q000639:trends; D017510:Protein Folding; D017433:Protein Structure, Secondary; D011506:Proteins / Q000737:chemistry*
chemical_list: D000682:Amyloid; D046911:Macromolecular Substances; D011506:Proteins