Ion-specific control of the self-assembly dynamics of a nanostructured protein lattice.

ABSTRACT: Self-assembling proteins offer a potential means of creating nanostructures with complex structure and function. However, using self-assembly to create nanostructures with long-range order whose size is tunable is challenging, because the kinetics and thermodynamics of protein interactions depend sensitively on solution conditions. Here we systematically investigate the impact of varying solution conditions on the self-assembly of SbpA, a surface-layer protein from Lysinibacillus sphaericus that forms two-dimensional nanosheets. Using high-throughput light scattering measurements, we mapped out diagrams that reveal the relative yield of self-assembly of nanosheets over a wide range of concentrations of SbpA and Ca(2+). These diagrams revealed a localized region of optimum yield of nanoshee

SUBMITTER: Rad B 

PROVIDER: S-EPMC4310639 | biostudies-literature | 2015 Jan

REPOSITORIES: biostudies-literature