Designing supramolecular protein assemblies Export

@article{Yeates2002, 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.}, author = {Yeates, T.}, citeulike-article-id = {6060737}, citeulike-linkout-0 = {http://dx.doi.org/10.1016/S0959-440X(02)00350-0}, citeulike-linkout-1 = {http://linkinghub.elsevier.com/retrieve/pii/S0959-440X(02)00350-0}, day = {1}, doi = {10.1016/S0959-440X(02)00350-0}, issn = {0959440X}, journal = {Current Opinion in Structural Biology}, keywords = {proteins, review, self-assembly}, month = {August}, number = {4}, pages = {464--470}, posted-at = {2009-11-03 17:03:18}, priority = {2}, title = {Designing supramolecular protein assemblies}, url = {http://dx.doi.org/10.1016/S0959-440X(02)00350-0}, volume = {12}, year = {2002} }

TY - JOUR ID - Yeates2002 L3 - citeulike-article-id:6060737 N2 - 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. IS - 4 JF - Current Opinion in Structural Biology SN - 0959440X EP - 470 TI - Designing supramolecular protein assemblies VL - 12 SP - 464 KW - proteins KW - review KW - self-assembly AU - Yeates, T PY - 2002/08/01/ UR - http://dx.doi.org/10.1016/S0959-440X(02)00350-0 ER -