(173q) Understanding Protein Mediated Biomineralization Using Cryogenic Electron Microscopy

Biomineralization refers to the process by which living organisms facilitate the formation of minerals, and proteins have been found to be the main mediating agents responsible for biomineralization (1). Elucidating the underlying molecular interactions behind biomineralization is important for fully understanding the fundamental mechanisms responsible, and ultimately harnessing these mechanisms for the design of hybrid biological-nanomaterial systems. Presently, there is a dearth of high resolution structural models of protein- inorganic NP (nanoparticle) interactions (2). Cryogenic electron microscopy or cryo-EM is a structural biology technique that has been used to obtain very high resolution structures of proteins including visualization of individual atoms (3). Cryo-EM can image proteins in their native state and functional environment. In this study we demonstrate the ability of cryo-EM as a promising powerful tool to study the protein - NP interface in biomineralization. We analyzed two systems ; GroEL -Platinum NP complex and Ferritin - Iron NP complex.

REFERENCES:

1. Wang, L. & Nilsen-Hamilton, M (2013), “Biomineralization proteins: From vertebrates to bacteria”, Frontiers in Biology 8(2), 234–246.
2. Weidner, T.; Castner, D. G. (2013), “SFG analysis of surface bound proteins: a route towards structure determination”, Phys Chem Chem Phys , 15 (30), 12516-24.
3. Yip, K.M., Fischer, N., Paknia, E. et al (2020), “Atomic-resolution protein structure determination by cryo-EM”, Nature 587, 157–161.