= G. R. Stark
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<G. R. Stark> coauthored, with <G. E. Davies>, a 1970 experiment using <protein cross-linking> to investigate the organization of oligomeric <proteins>. The method connected a chemical intervention to a measurable series of <protein subunit> masses.<Use of dimethyl suberimidate, a cross-linking reagent, in studying the subunit structure of oligomeric proteins by G. E. Davies and G. R. Stark>[Original byline and Abstract]{ref}
After reaction with <dimethyl suberimidate>, detergent <gel electrophoresis> separated individual chains and covalently linked combinations. The experiments included assemblies with identical subunits and assemblies containing different kinds of subunits; the latter showed unequal chemical reactivities.<Use of dimethyl suberimidate, a cross-linking reagent, in studying the subunit structure of oligomeric proteins by G. E. Davies and G. R. Stark>[Abstract: product series and dissimilar-protomer comparisons]{ref}
The unequal-reactivity observation gives an important interpretive control. Failure to observe a linked pair need not mean that its members were far apart in the native <protein>: reactive groups may have been inaccessible or poorly reactive. Chemical proximity measurements must therefore be interpreted together with the chemistry used to record them.
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