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Proteins can be crosslinked by chemical compounds without any accompanying change in the complicated three‐dimensional structure. Many bifunctional reagents that can react with functional groups in the side chains of the amino acids are now known. Not only can the distance between the linked amino acid residues be deduced from the known length of the bridge introduced, but information can also be obtained concerning changes in conformation during other reactions and concerning the arrangement of the components of a quaternary structure.
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Fasold et al. (1971) studied this question.
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