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Because of the relatively low cost compared to NMR instrumentation and ability to work on a wide range of proteins and under diverse conditions providing a wealth of structural information (such as the secondary and tertiary structures of proteins in solution, as well as details about protein folding, interactions, and conformational changes induced by environmental factors or ligand binding) by using relatively small amounts of protein sample, spectropolrimetry became a very popular technique, and spectropolarimeters are commonly found in many structural biology laboratories
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