Introduction to Our Research
Analysis of Protein Interaction Dynamics
Proteins assemble and disassemble to perform sophisticated functions. To understand protein functionality at the molecular level, it is necessary to investigate the structural changes of individual proteins and the modulation of protein–protein interactions in the presence of multiple proteins. We have developed new approaches for analyzing the dynamics of a multicomponent equilibrium system, a longstanding challenge in our field. Our approaches have enabled us to explore the molecular mechanisms and dynamics involved in signal transmission, protein transport, axon elongation, and other areas related to drug discovery.
- Development of an auto-sampling system designed for micro-flow small-angle X-ray scattering titration
(Poster presentation at the 2015 PF Symposium. Access restricted to authorized individuals only.)
Development of New Molecular Composite Materials
Silk and many other naturally-occurring functional materials are made of protein. Natural silk fibers have features that cannot be replaced by artificial products. Because proteins can be readily modified by changing their amino acid residues, artificial silk proteins represent a promising next-generation material. We are developing new protein-based materials that have properties superior to those of natural products. To this end, we focus on the self-assembly potential of protein. We investigate the elementary steps of protein self-organization and translate the findings into practical application.
Elucidating the Mechanisms of Protein Interaction Dynamics to Create Artificial Proteins
Dynamic protein self-assembly processes are regulated by the movements of the individual molecules involved. In particular, proton transfer within a protein molecule is considered to be a critical factor in its structural changes. Proteins can be viewed as a proton bioelectronics (protonics) device (Figure 4). We aim to clarify the mechanisms involved in protein self-assembly, and to use this knowledge to create artificial self-organizing proteins.