Our Investigations
Welcome to Jim DeYoreo’s laboratory, part of The Molecular Foundry, and the Materials Sciences Division at Lawrence Berkeley National Laboratory.
Our research group investigates the physics of aggregation, assembly and crystallization in biomolecular, biomineral and biomimetic systems. We also develop technology platforms for manipulating these processes. To investigate structural evolution and system dynamics, we use in situ microscopy and spectroscopy techniques including atomic force microscopy and spectroscopy, transmission electron microscopy and X-ray absorption spectroscopy. To manipulate nucleation and assembly we use scanned probe patterning and micro-contact printing to create nano-scale chemical templates, which define specific interactions with both inorganic and macromolecular targets.
Potential Impact
This research has the potential to impact a broad array of both scientific and technological challenges. Both biomineral formation and protein self-assembly are critical processes in human health and pathogenesis. The mineralized skeletons of marine organisms hold a record of the interplay between earth systems and biota over geologic timescales. Solutions to the challenge of capturing and sequestering carbon stand to benefit from knowledge of the control mechanisms exerted by these organisms during mineralization. Likewise, understanding the principles that control crystallization and assembly in biomolecular and biomineral systems inspire new approaches to tailored synthesis of functional materials. As a consequence of this diversity, our research group is highly collaborative and works with partners from the biological, geological and chemical sciences.
Four Research Areas
The research in our group falls into four main categories, each of which involves materials formation or assembly at surfaces in solutions and generally include organic-inorganic interfaces. We investigate peptide- and protein-mineral interactions to understand their role in biomineral
formation and to define the mechanisms by which these interactions can be used to direct growth of synthetic crystals. In parallel, we study the pathways of protein aggregation and self-assembly in the context of both functional and pathological tissue formation. Using surface functionalization and patterning, our group creates templates to direct nucleation of inorganic crystals, both as a means to investigate the underlying, structure, thermodynamic and kinetic controls and to develop a toolbox for manufacturing nanowires and quantum dots. Finally, we combine scanned probe patterning and site-specific mutagenesis to direct the organization of the viral capsids at surfaces, force spectroscopy to relate the dynamics of organization to the intermolecular interactions and Monte Carlo simulations to test physical models of directed organization.
Welcome to Jim DeYoreo’s laboratory, part of The Molecular Foundry, and the Materials Sciences Division at Lawrence Berkeley National Laboratory.
Potential Impact
This research has the potential to impact a broad array of both scientific and technological challenges. Both biomineral formation and protein self-assembly are critical processes in human health and pathogenesis. The mineralized skeletons of marine organisms hold a record of the interplay between earth systems and biota over geologic timescales. Solutions to the challenge of capturing and sequestering carbon stand to benefit from knowledge of the control mechanisms exerted by these organisms during mineralization. Likewise, understanding the principles that control crystallization and assembly in biomolecular and biomineral systems inspire new approaches to tailored synthesis of functional materials. As a consequence of this diversity, our research group is highly collaborative and works with partners from the biological, geological and chemical sciences.
Four Research Areas
The research in our group falls into four main categories, each of which involves materials formation or assembly at surfaces in solutions and generally include organic-inorganic interfaces. We investigate peptide- and protein-mineral interactions to understand their role in biomineral