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The conformational changes induced in concanavalin A by the binding of Mn++, Ca++, and alpha-methyl-D-mannoside have been studied at pH 5.28 by stopped flow nuclear magnetic resonance techniques. Three distinct conformation states of the protein have been kinetically observed and an ordered binding mechanism elucidated from a detailed analysis of the reaction records. In addition, the individual steps of this mechanism are interpreted in terms of molecular parameters characterizing the conformational states involved such as ligand exchange rates to the paramagnetic Mn++.
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Grimaldi et al. (1975) studied this question.
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