Russell F. Doolittle 2026-11-05
Russell F. Doolittle was a researcher in protein structure and molecular evolution at UC San Diego. His investigations connected the chemistry of fibrinogen and fibrinopeptides with comparisons of inherited molecular differences among species.[ref]
Russell Doolittle in University of California In Memoriam. Memorial: fibrinopeptide comparisons, fibrinogen studies and evolutionary relationships
With Andrew P. Laudano, Russell F. Doolittle tested synthetic peptides resembling the exposed ends of fibrin chains. Gly-Pro-Arg-Pro bound fibrinogen and its distal fragment D and inhibited fibrin polymerization, helping locate a binding interaction involved in assembly.[ref]
Synthetic peptide derivatives that bind to fibrinogen and prevent the polymerization of fibrin monomers by Andrew P. Laudano and Russell F. Doolittle. Abstract: synthetic peptides, fragment binding and inhibition
The experiment gives a small molecule an explanatory role: an imitation of one binding element can occupy a site without connecting two full-sized molecules. Interrupting network formation in this way tests a specific molecular contact. The same interest in protein sequences also supports a different kind of inference: comparing related molecules across species can reveal evolutionary relationships.