We demonstrate tracking of protein structural changes with time-resolved wide-angle X-ray scattering (TR-WAXS) with nanosecond time resolution. We investigated the tertiary and quaternary conformational changes of human hemoglobin under nearly physiological conditions triggered by laser-induced ligand photolysis. We also report data on optically induced tertiary relaxations of myoglobin and refolding of cytochrome c to illustrate the wide applicability of the technique. By providing insights into the structural dynamics of proteins functioning in their natural environment, TR-WAXS complements and extends results obtained with time-resolved optical spectroscopy and X-ray crystallography.
CAMMARATA, M., LEVANTINO, M., SCHOTTE, F., ANFINRUD, P.A., EWALD, F., CHOI, J., et al. (2008). Tracking the structural dynamics of proteins in solution using time-resolved wide-angle X-ray scattering. NATURE METHODS, 5(10), 881-886 [10.1038/nmeth.1255].
Tracking the structural dynamics of proteins in solution using time-resolved wide-angle X-ray scattering
LEVANTINO, Matteo;CUPANE, Antonio;
2008-01-01
Abstract
We demonstrate tracking of protein structural changes with time-resolved wide-angle X-ray scattering (TR-WAXS) with nanosecond time resolution. We investigated the tertiary and quaternary conformational changes of human hemoglobin under nearly physiological conditions triggered by laser-induced ligand photolysis. We also report data on optically induced tertiary relaxations of myoglobin and refolding of cytochrome c to illustrate the wide applicability of the technique. By providing insights into the structural dynamics of proteins functioning in their natural environment, TR-WAXS complements and extends results obtained with time-resolved optical spectroscopy and X-ray crystallography.
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