Visualization of Iron-Binding Micelles in Acidic Recombinant Biomineralization Protein, MamC Kashyap, Sanjay Valverde-Tercedor, Carmen Sánchez-Quesada, Miguel Jiménez López, Concepción Prozorov, Tanya Transmission electron microscopy In situ TEM Surface patterning tools Magnetotactic bacteria Magnetosome membrane Proteomic analysis Nanoparticles MMS6 Nanocrystal Ferritin Biological macromolecules are utilized in low-temperature synthetic methods to exert precise control over nanoparticle nucleation and placement. They enable low-temperature formation of a variety of functional nanostructured materials with properties often not achieved via conventional synthetic techniques. Here we report on the in situ visualization of a novel acidic bacterial recombinant protein, MamC, commonly present in the magnetosome membrane of several magnetotactic bacteria, including Magnetococcus marinus, strain MC-1. Our findings provide an insight into the self-assembly of MamC and point to formation of the extended protein surface, which is assumed to play an important role in the formation of biotemplated inorganic nanoparticles. The self-organization of MamC is compared to the behavior of another acidic recombinant iron-binding protein, Mms6. 2014-05-23T11:36:52Z 2014-05-23T11:36:52Z 2014 info:eu-repo/semantics/article Kashyap, S.; et al. Visualization of Iron-Binding Micelles in Acidic Recombinant Biomineralization Protein, MamC. Journal of Nanomaterials, 2014: 320124 (2014). [http://hdl.handle.net/10481/31888] 1687-4110 1687-4129 http://hdl.handle.net/10481/31888 10.1155/2014/320124 eng http://creativecommons.org/licenses/by-nc-nd/3.0/ info:eu-repo/semantics/openAccess Creative Commons Attribution-NonCommercial-NoDerivs 3.0 License Hindawi Publishing Corporation