Computational and experimental studies of collagen and related diseases

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.

Department dc:contributor.department

Massachusetts Institute of Technology. Dept. of Electrical Engineering and Computer Science.

Grantor dc:publisher

Massachusetts Institute of Technology

Year dc:date.issued

2005

Author dc:creator

• Yang, Chen, M. Eng. Massachusetts Institute of Technology

Advisor dc:contributor.advisor

• Collin M. Stultz.

• Electrical Engineering and Computer Science.

Statement dc:rights

• M.I.T. theses are protected by copyright. They may be viewed from this source for any purpose, but reproduction or distribution in any format is prohibited without written permission. See provided URL for inquiries about permission.

Licence dc:rights.uri

• http://dspace.mit.edu/handle/1721.1/7582

Language dc:language.iso

eng

Handle dc:identifier.uri

http://hdl.handle.net/1721.1/37058

OAI identifier oai:identifier

oai:dspace.mit.edu:1721.1/37058