Computational and experimental studies of collagen and related diseases
Name
82461273-MIT.pdf
Description
Full printable version
Size
20.06 MB
Format
Adobe PDF
Checksum (MD5)
43a739610728c782e1e39a9a2a616339
Author(s)
Yang, Chen, M. Eng. Massachusetts Institute of Technology
Advisor(s)
Collin M. Stultz.
Date Issued
2005
Publisher
Massachusetts Institute of Technology
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.
Description
Thesis (M. Eng. and S.B.)--Massachusetts Institute of Technology, Dept. of Electrical Engineering and Computer Science, 2005.
Page 86 blank.
Includes bibliographical references (p. 83-85).
Subjects
Electrical Engineering and Computer Science.
MIT Department
Massachusetts Institute of Technology. Department of Electrical Engineering and Computer Science
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