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Full-Text Articles in Physics

Self-Assembly And Biphasic Iron-Binding Characteristics Of Mms6, A Bacterial Protein That Promotes The Formation Of Superparamagnetic Magnetite Nanoparticles Of Uniform Size And Shape, Lijun Wang, Tanya Prozorov, Pierre E. Palo, Xunpei Liu, David Vaknin, Ruslan Prozorov, Surya K. Mallapragada, Marit Nilsen-Hamilton Jan 2012

Self-Assembly And Biphasic Iron-Binding Characteristics Of Mms6, A Bacterial Protein That Promotes The Formation Of Superparamagnetic Magnetite Nanoparticles Of Uniform Size And Shape, Lijun Wang, Tanya Prozorov, Pierre E. Palo, Xunpei Liu, David Vaknin, Ruslan Prozorov, Surya K. Mallapragada, Marit Nilsen-Hamilton

Chemical and Biological Engineering Publications

Highly ordered mineralized structures created by living organisms are often hierarchical in structure with fundamental structural elements at nanometer scales. Proteins have been found responsible for forming many of these structures, but the mechanisms by which these biomineralization proteins function are generally poorly understood. To better understand its role in biomineralization, the magnetotactic bacterial protein, Mms6, which promotes the formation in vitro of superparamagnetic magnetite nanoparticles of uniform size and shape, was studied for its structure and function. Mms6 is shown to have two phases of iron binding: one high affinity and stoichiometric and the other low affinity, high capacity ...