<?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>2026-09-19T10:31:46Z</responseDate><request verb="GetRecord" identifier="oai:dspace.mit.edu:1721.1/28707" metadataPrefix="dim">https://dspace.mit.edu/server/oai/request</request><GetRecord><record><header><identifier>oai:dspace.mit.edu:1721.1/28707</identifier><datestamp>2022-01-13T07:54:21Z</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">Bernhardt L. Trout.</dim:field>
   <dim:field mdschema="dc" element="contributor" qualifier="author" lang="en_US">Chang, Nai-yuan, 1973-</dim:field>
   <dim:field mdschema="dc" element="contributor" qualifier="other" lang="en_US">Massachusetts Institute of Technology. Dept. of Chemistry.</dim:field>
   <dim:field mdschema="dc" element="contributor" qualifier="department">Massachusetts Institute of Technology. Department of Chemistry</dim:field>
   <dim:field mdschema="dc" element="date" qualifier="accessioned">2005-09-27T17:53:49Z</dim:field>
   <dim:field mdschema="dc" element="date" qualifier="available">2005-09-27T17:53:49Z</dim:field>
   <dim:field mdschema="dc" element="date" qualifier="copyright" lang="en_US">2004</dim:field>
   <dim:field mdschema="dc" element="date" qualifier="issued" lang="en_US">2004</dim:field>
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   <dim:field mdschema="dc" element="identifier" qualifier="oclc" lang="en_US">59133389</dim:field>
   <dim:field mdschema="dc" element="description" lang="en_US">Thesis (S.M.)--Massachusetts Institute of Technology, Dept. of Chemistry, 2004.</dim:field>
   <dim:field mdschema="dc" element="description" lang="en_US">Includes bibliographical references (leaf 26).</dim:field>
   <dim:field mdschema="dc" element="description" qualifier="abstract" lang="en_US">In this study, thermodynamic integration and molecular dynamics methods were used to elucidate the factors affecting stabilities of collagen-like peptides. We proposed to investigate three specific aspects: (1) the stabilizing effect of hydroxyproline (Hyp), (2) the destabilizing effect of replacing Gly, and (3) the role of water mediated hydrogen bonds. A better understanding of the origins of the stabilities of collagens will help in the design of new biomaterials and the treatment of collagen-related diseases.</dim:field>
   <dim:field mdschema="dc" element="description" qualifier="statementofresponsibility" lang="en_US">by Nai-yuan Chang.</dim:field>
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   <dim:field mdschema="dc" element="publisher" lang="en_US">Massachusetts Institute of Technology</dim:field>
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   <dim:field mdschema="dc" element="subject" lang="en_US">Chemistry.</dim:field>
   <dim:field mdschema="dc" element="title" lang="en_US">Computational studies on the factors influencing stabilities of collagen-like peptides</dim:field>
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   	&lt;Title>Computational studies on the factors influencing stabilities of collagen-like peptides&lt;/Title>
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   	&lt;PublicationDate>2004&lt;/PublicationDate>
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    &lt;Keyword>Chemistry.&lt;/Keyword>
   	&lt;Abstract>In this study, thermodynamic integration and molecular dynamics methods were used to elucidate the factors affecting stabilities of collagen-like peptides. We proposed to investigate three specific aspects: (1) the stabilizing effect of hydroxyproline (Hyp), (2) the destabilizing effect of replacing Gly, and (3) the role of water mediated hydrogen bonds. A better understanding of the origins of the stabilities of collagens will help in the design of new biomaterials and the treatment of collagen-related diseases.&lt;/Abstract>
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