Protein Conformation in Solution: Cross-Linking of Lysozyme

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Science  12 Jan 1968:
Vol. 159, Issue 3811, pp. 210-211
DOI: 10.1126/science.159.3811.210


The cross-linking of lysozyme by reaction with phenol-2,4-disulfonyl chloride has been effected. The cross-linked protein retained enzymatic activity, has approximately the same molecular weight as native lysozyme, and has essentially the same conformation as native lysozyme as judged by optical rotatory dispersion analysis. The positions of sulfonylation were assigned by a standard degradation sequence; the presence of sulfonamide bonds was confirmed by infrared spectroscopy. Cross-links may thus be introduced without incurring major structural changes in the protein, and certain intramolecular distances that are allowed in the active enzyme may be deduced.

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