Journal
SCIENTIFIC REPORTS
Volume 7, Issue -, Pages -Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/s41598-017-14022-7
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Funding
- Scientific Research on Innovative Areas 3D Active-Site Science [26105005 2604]
- AMED-CREST - Japan Agency of Medical Research (AMED)
- Japan Society for the Promotion of Science (JSPS) [26-7839]
- JSPS through the Program for Leading Graduate Schools (MERIT)
- Grants-in-Aid for Scientific Research [15H04362, 26105001, 17H06352, 15K21719, 26105005] Funding Source: KAKEN
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Proteins in solution are conventionally considered macromolecules. Dynamic microscopic structures in supersaturated protein solutions have received increasing attention in the study of protein crystallisation and the formation of misfolded aggregates. Here, we present a method for observing rotational dynamic structures that can detect the interaction of nanoscale lysozyme protein networks via diffracted X-ray tracking (DXT). Our DXT analysis demonstrated that the rearrangement behaviours of lysozyme networks or clusters, which are driven by local density and concentration fluctuations, generate force fields on the femtonewton to attonewton (fN - aN) scale. This quantitative parameter was previously observed in our experiments on supersaturated inorganic solutions. This commonality provides a way to clarify the solution structures of a variety of supersaturated solutions as well as to control nucleation and crystallisation in supersaturated solutions.
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