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FUJISAWA Tetsuro |
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Title |
Professor
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Department |
Department of Chemistry and Biomolecular Science |
Course |
Biomolecular Science Course |
Research fields
Most protein consists of several polypeptides and often associates/dissociates with each other when it functions as an enzyme. In order to clarify this dynamical view of protein complex, it is essential to measure the change of its shape in solution. However, it is not straightforward because there exists many structural states of protein in a given solution. My research attempts to extract the individuals from the ensemble of protein structures by combinational use of synchrotron small-angle scattering and hydrostatic pressure techniques: the former measures the global structure of protein and the latter shfts the equilibrium of the structure states.
My recent research focuses on the structure-function relationship of an industrial protein that hydrolyzes nitrile compounds. In addition, since my research needs to embed carry-in instruments into the synchrotron facility, embedding software as well as data analysis software have been developed.
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Fig. 1 Pressure shift of association equilibrium |
Fig. 2 Setup for high pressure synchrotron SAS (BL45XU@Spring-8) |
Research Keywords
Synchrotron small-angle scattering
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High hydrostatic pressure
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Protein complex structure
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Data collection and analysis
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