<?xml version="1.0" encoding="UTF-8"?><?xml-stylesheet type="text/xsl" href="static/style.xsl"?><OAI-PMH xmlns="http://www.openarchives.org/OAI/2.0/" xmlns:xsi="http://www.w3.org/2001/XMLSchema-instance" xsi:schemaLocation="http://www.openarchives.org/OAI/2.0/ http://www.openarchives.org/OAI/2.0/OAI-PMH.xsd"><responseDate>2026-09-20T20:23:25Z</responseDate><request verb="GetRecord" identifier="oai:dspace.mit.edu:1721.1/37058" metadataPrefix="dim">https://dspace.mit.edu/server/oai/request</request><GetRecord><record><header><identifier>oai:dspace.mit.edu:1721.1/37058</identifier><datestamp>2026-06-06T01:04:24Z</datestamp><setSpec>com_1721.1_7582</setSpec><setSpec>com_1721.1_7581</setSpec><setSpec>col_1721.1_131023</setSpec></header><metadata><dim:dim xmlns:dim="http://www.dspace.org/xmlns/dspace/dim" xmlns:xsi="http://www.w3.org/2001/XMLSchema-instance" xmlns:doc="http://www.lyncode.com/xoai" xsi:schemaLocation="http://www.dspace.org/xmlns/dspace/dim http://www.dspace.org/schema/dim.xsd">
   <dim:field mdschema="dc" element="contributor" qualifier="advisor" lang="en_US">Collin M. Stultz.</dim:field>
   <dim:field mdschema="dc" element="contributor" qualifier="author" lang="en_US">Yang, Chen, M. Eng. Massachusetts Institute of Technology</dim:field>
   <dim:field mdschema="dc" element="contributor" qualifier="other" lang="en_US">Massachusetts Institute of Technology. Dept. of Electrical Engineering and Computer Science.</dim:field>
   <dim:field mdschema="dc" element="contributor" qualifier="department">Massachusetts Institute of Technology. Department of Electrical Engineering and Computer Science</dim:field>
   <dim:field mdschema="dc" element="date" qualifier="accessioned">2007-04-03T17:07:14Z</dim:field>
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   <dim:field mdschema="dc" element="date" qualifier="copyright" lang="en_US">2005</dim:field>
   <dim:field mdschema="dc" element="date" qualifier="issued" lang="en_US">2005</dim:field>
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   <dim:field mdschema="dc" element="identifier" qualifier="oclc" lang="en_US">82461273</dim:field>
   <dim:field mdschema="dc" element="description" lang="en_US">Thesis (M. Eng. and S.B.)--Massachusetts Institute of Technology, Dept. of Electrical Engineering and Computer Science, 2005.</dim:field>
   <dim:field mdschema="dc" element="description" lang="en_US">Page 86 blank.</dim:field>
   <dim:field mdschema="dc" element="description" lang="en_US">Includes bibliographical references (p. 83-85).</dim:field>
   <dim:field mdschema="dc" element="description" qualifier="abstract" lang="en_US">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.</dim:field>
   <dim:field mdschema="dc" element="description" qualifier="statementofresponsibility" lang="en_US">by Chen Yang.</dim:field>
   <dim:field mdschema="dc" element="description" qualifier="degree" lang="en_US">M.Eng.</dim:field>
   <dim:field mdschema="dc" element="description" qualifier="degree" lang="en_US">S.B.</dim:field>
   <dim:field mdschema="dc" element="format" qualifier="extent" lang="en_US">86, i-xxxiii p.</dim:field>
   <dim:field mdschema="dc" element="language" qualifier="iso" lang="en_US">eng</dim:field>
   <dim:field mdschema="dc" element="publisher" lang="en_US">Massachusetts Institute of Technology</dim:field>
   <dim:field mdschema="dc" element="rights" lang="en_US">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.</dim:field>
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   <dim:field mdschema="dc" element="subject" lang="en_US">Electrical Engineering and Computer Science.</dim:field>
   <dim:field mdschema="dc" element="title" lang="en_US">Computational and experimental studies of collagen and related diseases</dim:field>
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   	&lt;Title>Computational and experimental studies of collagen and related diseases&lt;/Title>
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   	&lt;PublicationDate>2005&lt;/PublicationDate>
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   	&lt;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.&lt;/Abstract>
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