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As a result, fluorescence methods allow for detection and analysis of rapid, local motions, such as fluctuations of individual amino acid side chains and the local relaxation of the protein matrix (10 -12 to 10 -9 s), capturing structural changes, such as domain motions or transitions between different protein states (10 -6 to 10 -3 s), as well as analysis of slower, large-scale motions and conformational changes, ranging from folding-unfolding processes to binding or dissociation of other molecules (10 -3 s to minutes)