Computational and experimental studies of collagen and related diseases

Abstract

Collagen is the most abundant proteins in mammals, and collagen degradation is a process that may be associated with many diseases. In this research we use collagen-like peptides that model both cleavage and noncleavage sites of collagen type III to study the stability and degradation of collagen as a function of amino acid sequence variation. Molecular Dynamics is used to compute the potential of mean force of these collagen-like peptides and predict their triple helical content. The predicted result is then compared with experimental results from Circular Dichroism spectroscopy. Similar studies are done on mutant peptides of collagen from the Ehlers-Danlos Syndrome type IV.