Interacting Sites in Novel Polymeric Proteins.
Final rept. 1 Aug 91-31 Mar 95,
MISSISSIPPI UNIV MEDICAL CENTER JACKSON
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Protein-protein and intraprotein interactions were studied in natural, recombinant and synthetic domains of proteins that form aquatic silk. Subsets of natural proteins were found to associate into discrete high molecular mass complexes thought to be the non-covalent precursors to insoluble silk. A recombinant protein mimicking a single core repeat from a 1000-kDa silk protein reversibly formed two intramolecular disulfide bonds however, more than one comformation existed. A synthetic peptide encompassing all four cysteines also formed intramolecular disulfide bonds. The results obtained suggested new steps in the fiber formation pathway including properties of the recombinant protein that may render it useful as a degradable biomolecular material.
- Polymer Chemistry