hamon
Online ISSN : 1884-636X
Print ISSN : 1349-046X
ISSN-L : 1349-046X
Solution Structure of Proteins under High Hydrostatic Pressure Studied by Synchrotron Small-Angle X-ray Scattering
Tetsuro Fujisawa
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2006 Volume 16 Issue 1 Pages 60-63

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Abstract
The use of high hydrostatic pressure has been a useful tool for studying physicochemical properties of proteins. Since proteins change their volume during reactions, pressure perturbs the equilibria and the relative populations, between the multiple conformers. We have been developing a high-pressure cell for HP-SAXS that has a small sample volume (ca. 0.05mL) and sufficiently high reproducibility, to collect solution scattering data from large protein complexes. We report the present status of the development and its application for large protein complex.
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© The Japanese Society for Neutron Science
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