<?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>2026-09-19T01:45:59Z</responseDate><request verb="GetRecord" identifier="oai:dspace.mit.edu:1721.1/127906" metadataPrefix="dim">https://dspace.mit.edu/server/oai/request</request><GetRecord><record><header><identifier>oai:dspace.mit.edu:1721.1/127906</identifier><datestamp>2026-06-16T18:54:40Z</datestamp><setSpec>com_1721.1_7582</setSpec><setSpec>com_1721.1_7581</setSpec><setSpec>col_1721.1_131022</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">Julia H. Ortony.</dim:field>
   <dim:field mdschema="dc" element="contributor" qualifier="author" lang="en_US">Lindemann, William Robin.</dim:field>
   <dim:field mdschema="dc" element="contributor" qualifier="other" lang="en_US">Massachusetts Institute of Technology. Department of Materials Science and Engineering.</dim:field>
   <dim:field mdschema="dc" element="contributor" qualifier="department" lang="en_US">Massachusetts Institute of Technology. Department of Materials Science and Engineering</dim:field>
   <dim:field mdschema="dc" element="date" qualifier="accessioned">2020-10-08T21:29:45Z</dim:field>
   <dim:field mdschema="dc" element="date" qualifier="available">2020-10-08T21:29:45Z</dim:field>
   <dim:field mdschema="dc" element="date" qualifier="copyright" lang="en_US">2020</dim:field>
   <dim:field mdschema="dc" element="date" qualifier="issued" lang="en_US">2020</dim:field>
   <dim:field mdschema="dc" element="identifier" qualifier="uri">https://hdl.handle.net/1721.1/127906</dim:field>
   <dim:field mdschema="dc" element="identifier" qualifier="oclc" lang="en_US">1197629010</dim:field>
   <dim:field mdschema="dc" element="description" lang="en_US">Thesis: Ph. D., Massachusetts Institute of Technology, Department of Materials Science and Engineering, May, 2020</dim:field>
   <dim:field mdschema="dc" element="description" lang="en_US">Cataloged from the official PDF of thesis.</dim:field>
   <dim:field mdschema="dc" element="description" lang="en_US">Includes bibliographical references (pages 161-179).</dim:field>
   <dim:field mdschema="dc" element="description" qualifier="abstract" lang="en_US">In solutions, the dynamic behavior of soft materials is often critical to their function. In biological materials such as proteins and peptides, the edict that 'structure dictates function' has been supplanted in recent decades by recognition that features like intrinsic disorder, conformational distribution, and solvent dynamics often play a part which is equally fundamental to the binding and reactivity of these materials. The same revelation holds for many other functional soft materials, including abiotic peptides and self-assembling materials, where function is controlled by the dynamic behavior of both the compound and the substrate. In this work, I elucidate the role of dynamics in several significant functional polyamides by the synthesis and characterization of samples spin-labeled for electron paramagnetic resonance (EPR) spectroscopy. By this approach, I developed insight into several soft-materials systems, including abiotic peptide tags, combinatorially selected for bioconjugation; fibronectin mimetic peptides, designed for therapeutic purposes, biomaterials and drug delivery; and finally, novel, self-assembling polyamide materials designed for water purification and energy conservation.</dim:field>
   <dim:field mdschema="dc" element="description" qualifier="statementofresponsibility" lang="en_US">by William Robin Lindemann.</dim:field>
   <dim:field mdschema="dc" element="description" qualifier="degree" lang="en_US">Ph.D.</dim:field>
   <dim:field mdschema="dc" element="description" qualifier="collection" lang="en_US">Ph.D. Massachusetts Institute of Technology, Department of Materials Science and Engineering</dim:field>
   <dim:field mdschema="dc" element="format" qualifier="extent" lang="en_US">179 pages</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">MIT theses may be protected by copyright. Please reuse MIT thesis content according to the MIT Libraries Permissions Policy, which is available through the URL provided.</dim:field>
   <dim:field mdschema="dc" element="rights" qualifier="uri" lang="en_US">http://dspace.mit.edu/handle/1721.1/7582</dim:field>
   <dim:field mdschema="dc" element="subject" lang="en_US">Materials Science and Engineering.</dim:field>
   <dim:field mdschema="dc" element="title" lang="en_US">Dynamics characterization for designing functional soft materials</dim:field>
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   	&lt;Title>Dynamics characterization for designing functional soft materials&lt;/Title>
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   	&lt;PublicationDate>2020&lt;/PublicationDate>
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    &lt;Keyword>Materials Science and Engineering.&lt;/Keyword>
   	&lt;Abstract>In solutions, the dynamic behavior of soft materials is often critical to their function. In biological materials such as proteins and peptides, the edict that &amp;apos;structure dictates function&amp;apos; has been supplanted in recent decades by recognition that features like intrinsic disorder, conformational distribution, and solvent dynamics often play a part which is equally fundamental to the binding and reactivity of these materials. The same revelation holds for many other functional soft materials, including abiotic peptides and self-assembling materials, where function is controlled by the dynamic behavior of both the compound and the substrate. In this work, I elucidate the role of dynamics in several significant functional polyamides by the synthesis and characterization of samples spin-labeled for electron paramagnetic resonance (EPR) spectroscopy. By this approach, I developed insight into several soft-materials systems, including abiotic peptide tags, combinatorially selected for bioconjugation; fibronectin mimetic peptides, designed for therapeutic purposes, biomaterials and drug delivery; and finally, novel, self-assembling polyamide materials designed for water purification and energy conservation.&lt;/Abstract>
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