Real time study of protein dynamics during a non-classical crystallization process
Protein crystallization is of great interest due to its crucial role for the determination of protein structures, as well as in other fields such as drug engineering by pharmaceutical industries [J. Gunton et al. Protein Condensation: Kinetic Pathways to Crystallization and Disease. CUP, (2007)]. Despite its importance, a fundamental understanding of the mechanisms underlying such a process is still missing. Recently, both experimental [F. Zhang et al. Journal of Applied Crystallography 44, (2011); A.Sauter et al., J.Am.Chem.Soc. 137, 1485 (2015)] and theoretical [P. G. Vekilov, Nanoscale 2, (2010)] studies have shown that, under certain conditions, crystallization follows a multi-step mechanism, rather than the classical nucleation pathway. In order to gain a better understanding of such processes, an in situ study of the dynamics of a suitable crystallizing systems by QENS at IN11 may provide new extremely useful information, thus potentially significantly improving the general physical picture. This proposal continues the IN16B and IN11 work.
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GRIMALDO Marco; BECK Christian; CZAKKEL Orsolya; FEUSTEL Michal; ROOSEN RUNGE Felix; Frank Schreiber; SEYDEL Tilo; SOHMEN Benedikt and ZHANG Fajun. (2016). Real time study of protein dynamics during a non-classical crystallization process. Institut Laue-Langevin (ILL) doi:10.5291/ILL-DATA.8-04-766
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