{"id":{"repo_id":"vt","oai_identifier":"oai:vtechworks.lib.vt.edu:10919/50500"},"canonical_url":"https://search.dev.ndltd.org/etd/vt/oai:vtechworks.lib.vt.edu:10919/50500","repository":{"repo_id":"vt","name":"Virginia Tech","base_url":"https://vtechworks.lib.vt.edu/oai/request"},"display":{"title":"Non-equilibrium Dynamics of Nanoscale Soft Matter Deformation","abstract":"Life is soft. From the fluid-like structure of lipid bilayers to the flexible folding of proteins, the realm of nanoscale soft matter is a complex and vibrant area of research. The lure of personalized medicine, advanced sensing technology, and understanding life at a fundamental level pushes research forward. This work considers to areas: (1) lipid bilayer dynamics in the presence of substrate defects and (2) the inverse temperature transition of elastic proteins. Molecular dynamics simulations as well as umbrella sampling were employed. The behavior of the bilayers discussed in the work provides evidence that small defects on confining surfaces can promote nucleation of lipid tethers. Results the second part of this work indicate elastin-like peptides experiencing inverse temperature transitions may be capable of performing amounts of work similar to RNA polymerase; additionally, resilin's inverse temperature transition may be closely linked to the molecule's ability to efficiently transmit energy through the similar coil-β secondary structure transition seen in both cases. These insights into the inverse transition temperature are relevant for the design of bio-inspired sensors and energy storage devices.","abstract_html":"Life is soft. From the fluid-like structure of lipid bilayers to the flexible folding of proteins, the realm of nanoscale soft matter is a complex and vibrant area of research. The lure of personalized medicine, advanced sensing technology, and understanding life at a fundamental level pushes research forward. This work considers to areas: (1) lipid bilayer dynamics in the presence of substrate defects and (2) the inverse temperature transition of elastic proteins. Molecular dynamics simulations as well as umbrella sampling were employed. The behavior of the bilayers discussed in the work provides evidence that small defects on confining surfaces can promote nucleation of lipid tethers. Results the second part of this work indicate elastin-like peptides experiencing inverse temperature transitions may be capable of performing amounts of work similar to RNA polymerase; additionally, resilin's inverse temperature transition may be closely linked to the molecule's ability to efficiently transmit energy through the similar coil-β secondary structure transition seen in both cases. These insights into the inverse transition temperature are relevant for the design of bio-inspired sensors and energy storage devices.","abstract_has_math":false,"creators":["Fergusson, Austin D."],"institution":"Virginia Tech","degree_name":"Master of Science","degree_level":"masters","degree_discipline":"Engineering Mechanics","degree_department":"Engineering Science and Mechanics","school":null,"contributors":[],"advisors":[],"committee_chairs":["Holmes, Douglas P."],"committee_members":["Jung, Sunghwan","Staples, Anne E."],"year":2014,"date_issued":"2014-09-12","date_published":"2014-09-12","updated_at":"2026-07-22T22:20:27Z","subjects":["lipid bilayer","elastin","resilin","inverse temperature transition","umbrella sampling","potential of mean force"],"languages":[],"rights":["In Copyright"],"rights_urls":["http://rightsstatements.org/vocab/InC/1.0/"],"identifier_entries":[{"key":"dc:identifier.other","label":"Dc Identifier Other","values":["vt_gsexam:3545"],"render_values":[{"text":"vt_gsexam:3545","href":null,"code":true}]}]},"links":{"outbound_url":"http://hdl.handle.net/10919/50500","outbound_label":"Handle","outbound_source":"dc:identifier.uri"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:contributor.committeechair","label":"Committee Chair","values":["Holmes, Douglas P."]},{"key":"dc:contributor.committeemember","label":"Committee Member","values":["Jung, Sunghwan","Staples, Anne E."]},{"key":"dc:contributor.department","label":"Department","values":["Engineering Science and Mechanics"]},{"key":"dc:creator","label":"Author","values":["Fergusson, Austin D."]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date.accessioned","label":"Dc Date Accessioned","values":["2014-09-13T08:00:21Z"]},{"key":"dc:date.available","label":"Dc Date Available","values":["2014-09-13T08:00:21Z"]},{"key":"dc:date.issued","label":"Date","values":["2014-09-12"]},{"key":"dc:publisher","label":"Institution","values":["Virginia Tech"]},{"key":"dc:type","label":"Dc Type","values":["Thesis"]},{"key":"thesis:degree_discipline","label":"Discipline","values":["Engineering Mechanics"]},{"key":"thesis:degree_level","label":"Degree Level","values":["masters"]},{"key":"thesis:degree_name","label":"Degree Name","values":["Master of Science"]},{"key":"thesis:institution_name","label":"Thesis Institution Name","values":["Virginia Polytechnic Institute and State University"]}]},{"id":"subjects_keywords","label":"Subjects and Keywords","entries":[{"key":"dc:subject","label":"Dc Subject","values":["lipid bilayer","elastin","resilin","inverse temperature transition","umbrella sampling","potential of mean force"]}]},{"id":"language_rights","label":"Language and Rights","entries":[{"key":"dc:rights","label":"Dc Rights","values":["In Copyright"]},{"key":"dc:rights.uri","label":"Rights URI","values":["http://rightsstatements.org/vocab/InC/1.0/"]}]},{"id":"identifiers","label":"Identifiers","entries":[{"key":"dc:identifier.other","label":"Dc Identifier Other","values":["vt_gsexam:3545"]},{"key":"dc:identifier.uri","label":"Identifier URI","values":["http://hdl.handle.net/10919/50500"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description.abstract","label":"Abstract","values":["Life is soft. From the fluid-like structure of lipid bilayers to the flexible folding of proteins, the realm of nanoscale soft matter is a complex and vibrant area of research. The lure of personalized medicine, advanced sensing technology, and understanding life at a fundamental level pushes research forward. This work considers to areas: (1) lipid bilayer dynamics in the presence of substrate defects and (2) the inverse temperature transition of elastic proteins. Molecular dynamics simulations as well as umbrella sampling were employed. The behavior of the bilayers discussed in the work provides evidence that small defects on confining surfaces can promote nucleation of lipid tethers. Results the second part of this work indicate elastin-like peptides experiencing inverse temperature transitions may be capable of performing amounts of work similar to RNA polymerase; additionally, resilin's inverse temperature transition may be closely linked to the molecule's ability to efficiently transmit energy through the similar coil-β secondary structure transition seen in both cases. These insights into the inverse transition temperature are relevant for the design of bio-inspired sensors and energy storage devices."]},{"key":"dc:description.degree","label":"Dc Description Degree","values":["Master of Science"]},{"key":"dc:format.medium","label":"Dc Format Medium","values":["ETD"]},{"key":"dc:title","label":"Title","values":["Non-equilibrium Dynamics of Nanoscale Soft Matter Deformation"]}]}],"canonical_facts":{"dc:contributor.committeechair":["Holmes, Douglas P."],"dc:contributor.committeemember":["Jung, Sunghwan","Staples, Anne E."],"dc:contributor.department":["Engineering Science and Mechanics"],"dc:creator":["Fergusson, Austin D."],"dc:date.accessioned":["2014-09-13T08:00:21Z"],"dc:date.available":["2014-09-13T08:00:21Z"],"dc:date.issued":["2014-09-12"],"dc:description.abstract":["Life is soft. From the fluid-like structure of lipid bilayers to the flexible folding of proteins, the realm of nanoscale soft matter is a complex and vibrant area of research. 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