Abstract
Understanding of biological function requires knowledge both on structural and dynamical aspects. The aim of time-resolved X-ray diffraction is to combine structural and kinetic methods by monitoring structural or conformational changes within a single protein or assemblies of proteins during their biological action in real time. This requires (i) a powerful X-ray source, (ii) appropriate detectors capable of dealing with high local and total count rates and (iii) a suitable trigger mechanism. These aspects are briefly discussed with emphasis on light as trigger for initiation of structural or conformational changes. Examples are presented on muscle contraction, lipid• phase transitions, the photocycle of bacteriorhodopsin and the application of Laue crystallography on the protein p21. PACS numbers: 61.10.—i, 87.80.+s, 52.50.Jm
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