= T. D. Meek
{c}
<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.<Human immunodeficiency virus 1 protease expressed in Escherichia coli behaves as a dimeric aspartic protease by T. D. Meek and others>[Abstract; PNAS 86, 1841–1845, 1989]{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>.<Human immunodeficiency virus 1 protease expressed in Escherichia coli behaves as a dimeric aspartic protease by T. D. Meek and others>[Abstract: mass measurements, cross-linking and dimeric active enzyme]{ref}
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