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Article
Characterization of a highly flexible self-assembling protein system designed to form nanocages
Protein Science
(2014)
Abstract
The design of proteins that self-assemble into well-defined, higher order structures is an important goal that has potential applications in synthetic biology, materials science, and medicine. We previously designed a two-component protein system, designated A-(+) and A-(−), in which self-assembly is mediated by complementary electrostatic interactions between two coiled-coil sequences appended to the C-terminus of a homotrimeric enzyme with C3 symmetry. The coiled-coil sequences are attached through a short, flexible spacer sequence providing the system with a high degree of conformational flexibility. Thus, the primary constraint guiding which structures the system may assemble into is the symmetry of the protein building block.
Keywords
- coiled-coil,
- self-assembly,
- protein cages,
- symmetry,
- analytical ultracentrifugation,
- cryo-electron microscopy
Disciplines
Publication Date
2014
DOI
10.1002/pro.2405
Citation Information
Patterson, D. P., Su, M., Franzmann, T. M., Sciore, A., Skiniotis, G., & Marsh, E. N. G.
(2014). Characterization of a highly flexible self-assembling protein system designed to
form nanocages. Protein Science, 23, 190–199.