T. D. Meek is the first author of a 1989 study characterizing HIV-1 protease produced in Escherichia coli. The purified enzyme processed a viral precursor protein into fragments consistent with the expected mature products. The investigators also compared molecular masses under denaturing and nondenaturing conditions and used protein cross-linking to probe subunit association.[ref]
The apparent mass changed from about 11,000 to 22,000 between dissociated and associated conditions, consistent with a dimer. Cross-linking supplied a separate line of evidence for association. Pairing such structural measurements with an activity assay was important: a single chain observed under denaturing conditions need not be the functional unit of an active enzyme.[ref]
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