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   <dim:field mdschema="dc" element="contributor" qualifier="advisor" lang="en_US">Paul Matsudaira.</dim:field>
   <dim:field mdschema="dc" element="contributor" qualifier="author" lang="en_US">Muso, Taro M. (Taro Michael)</dim:field>
   <dim:field mdschema="dc" element="contributor" qualifier="other" lang="en_US">Harvard University--MIT Division of Health Sciences and Technology.</dim:field>
   <dim:field mdschema="dc" element="contributor" qualifier="department">Harvard University--MIT Division of Health Sciences and Technology</dim:field>
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   <dim:field mdschema="dc" element="date" qualifier="copyright" lang="en_US">2007</dim:field>
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   <dim:field mdschema="dc" element="identifier" qualifier="oclc" lang="en_US">181101692</dim:field>
   <dim:field mdschema="dc" element="description" lang="en_US">Thesis (S.M.)--Harvard-MIT Division of Health Sciences and Technology, 2007.</dim:field>
   <dim:field mdschema="dc" element="description" lang="en_US">Includes bibliographical references (p. 133-141).</dim:field>
   <dim:field mdschema="dc" element="description" qualifier="abstract" lang="en_US">Inquiry into intracellular and cytoskeletal mechanics requires an intracellular mechanical sensor to verify models of sub-cellular structure dynamics. To this end, the green fluorescent protein (GFP) is considered as a mechanical sensor candidate with many desirable characteristics. Implicit solvent molecular dynamics CHARMM simulations demonstrated details inaccessible by AFM and OT methods, such as the linkage dependency of fluorophore environment changes and the energy exchanges between protein components during protein unfolding. Theoretical considerations and in vitro experiments explored the parameters important to GFP conjugation by N-hydroxysuccinimide (NHS) ester chemistry, and the complexities associated with a polymer approach to a controlled distribution of force across fluorescent proteins in a polyacrylamide (PAM) gel.</dim:field>
   <dim:field mdschema="dc" element="description" qualifier="statementofresponsibility" lang="en_US">by Taro M. Muso.</dim:field>
   <dim:field mdschema="dc" element="description" qualifier="degree" lang="en_US">S.M.</dim:field>
   <dim:field mdschema="dc" element="format" qualifier="extent" lang="en_US">141 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>
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   <dim:field mdschema="dc" element="title" lang="en_US">Green fluorescent protein as a mechanical sensor</dim:field>
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   	&lt;Title>Green fluorescent protein as a mechanical sensor&lt;/Title>
   	&lt;Subtitle>GFP as a mechanical sensor&lt;/Subtitle>
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   	&lt;Abstract>Inquiry into intracellular and cytoskeletal mechanics requires an intracellular mechanical sensor to verify models of sub-cellular structure dynamics. To this end, the green fluorescent protein (GFP) is considered as a mechanical sensor candidate with many desirable characteristics. Implicit solvent molecular dynamics CHARMM simulations demonstrated details inaccessible by AFM and OT methods, such as the linkage dependency of fluorophore environment changes and the energy exchanges between protein components during protein unfolding. Theoretical considerations and in vitro experiments explored the parameters important to GFP conjugation by N-hydroxysuccinimide (NHS) ester chemistry, and the complexities associated with a polymer approach to a controlled distribution of force across fluorescent proteins in a polyacrylamide (PAM) gel.&lt;/Abstract>
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