= M. D. Pierschbacher
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<M. D. Pierschbacher> coauthored a 1984 experiment localizing a cell-attachment activity of <fibronectin> to a short <peptide>. With <E. Ruoslahti>, <M. D. Pierschbacher> showed that a synthetic four-residue sequence could reproduce the measured attachment-promoting activity.<Cell attachment activity of fibronectin can be duplicated by small synthetic fragments of the molecule by M. D. Pierschbacher and E. Ruoslahti>[Original byline and Abstract]{ref}
The sequence comprises <arginine>, <glycine>, <aspartate> and <serine>, often written RGDS. The experimentally tested four-residue <peptide> should be distinguished from the embedded <RGD motif> and from the entire <fibronectin> molecule.<Cell attachment activity of fibronectin can be duplicated by small synthetic fragments of the molecule by M. D. Pierschbacher and E. Ruoslahti>[Abstract: tetrapeptide identity and cell-attachment domain]{ref}
The experiment converts a broad observation into a molecular question. A large <protein> can contain many functional regions; a synthetic fragment tests whether one specified sequence is sufficient for a particular assay response. Reproducing that response does not establish that the fragment reproduces every function of <fibronectin>.
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