{"id":{"repo_id":"vt","oai_identifier":"oai:vtechworks.lib.vt.edu:10919/31829"},"canonical_url":"https://search.dev.ndltd.org/etd/vt/oai:vtechworks.lib.vt.edu:10919/31829","repository":{"repo_id":"vt","name":"Virginia Tech","base_url":"https://vtechworks.lib.vt.edu/oai/request"},"display":{"title":"Direct conversion of chemical energy to mechanical work using a phosphate charged protein","abstract":"Nature is able to convert chemical energy into mechanical work under modest conditions, i.e., physiological pH and ambient temperature and pressure. One of the most interesting systems is muscle modeled as the \"sliding filament\" system. The sliding filament system is a combination of a thin actin filament and a thick myosin filament that slide over one another by breaking the \"energy-rich\" pyrophosphate bond of ATP. The energy from ATP hydrolysis is used for mechanical motion and the energy lost during this process is used to heat our body. In biology, the sliding filament system is taken as a fairly effective model. For engineering systems, the energy lost to heat needs to be reduced to build an efficient energy converter. In our research, we use a phosphate charged protein, casein, and react it with divinyl sulfone (DVS) through a Michael addition reaction to produce a cross-linked gel. The protein gel could be ephosphorylated at standard conditions using bovine phosphatase (bp) and re-phosporylated using casein kinase. When attached to the protein, the negatively charged phosphate groups cause the gel to expand from repulsion. When removed, the protein contracts. Therefore, work is realized without sliding friction, which is the origin of the large energy loss in muscle. FT-IR spectroscopy allows us to follow the two biochemical reactions. We also show a thermodynamic analysis of the work and offer an estimation of the most basic term.","abstract_html":"Nature is able to convert chemical energy into mechanical work under modest conditions, i.e., physiological pH and ambient temperature and pressure. One of the most interesting systems is muscle modeled as the "sliding filament" system. The sliding filament system is a combination of a thin actin filament and a thick myosin filament that slide over one another by breaking the "energy-rich" pyrophosphate bond of ATP. The energy from ATP hydrolysis is used for mechanical motion and the energy lost during this process is used to heat our body. In biology, the sliding filament system is taken as a fairly effective model. For engineering systems, the energy lost to heat needs to be reduced to build an efficient energy converter. In our research, we use a phosphate charged protein, casein, and react it with divinyl sulfone (DVS) through a Michael addition reaction to produce a cross-linked gel. The protein gel could be ephosphorylated at standard conditions using bovine phosphatase (bp) and re-phosporylated using casein kinase. When attached to the protein, the negatively charged phosphate groups cause the gel to expand from repulsion. When removed, the protein contracts. Therefore, work is realized without sliding friction, which is the origin of the large energy loss in muscle. FT-IR spectroscopy allows us to follow the two biochemical reactions. We also show a thermodynamic analysis of the work and offer an estimation of the most basic term.","abstract_has_math":false,"creators":["Shen, Ying"],"institution":"Virginia Tech","degree_name":"Master of Science","degree_level":"masters","degree_discipline":"Biological Systems Engineering","degree_department":"Biological Systems Engineering","school":null,"contributors":[],"advisors":[],"committee_chairs":["Barone, Justin R."],"committee_members":["Senger, Ryan S.","Freeman, Joseph W."],"year":2010,"date_issued":"2010-04-09","date_published":"2010-04-09","updated_at":"2026-07-22T22:19:32Z","subjects":["re-phosphorylation","dephosphorylation","energy","protein gel","casein"],"languages":[],"rights":["In Copyright"],"rights_urls":["http://rightsstatements.org/vocab/InC/1.0/"],"identifier_entries":[{"key":"dc:identifier.other","label":"Dc Identifier Other","values":["etd-04222010-114302"],"render_values":[{"text":"etd-04222010-114302","href":null,"code":true}]}]},"links":{"outbound_url":"http://hdl.handle.net/10919/31829","outbound_label":"Handle","outbound_source":"dc:identifier.uri"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:contributor.committeechair","label":"Committee Chair","values":["Barone, Justin R."]},{"key":"dc:contributor.committeemember","label":"Committee Member","values":["Senger, Ryan S.","Freeman, Joseph W."]},{"key":"dc:contributor.department","label":"Department","values":["Biological Systems Engineering"]},{"key":"dc:creator","label":"Author","values":["Shen, Ying"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date.accessioned","label":"Dc Date Accessioned","values":["2014-03-14T20:34:02Z"]},{"key":"dc:date.available","label":"Dc Date Available","values":["2014-03-14T20:34:02Z","2010-05-25"]},{"key":"dc:date.issued","label":"Date","values":["2010-04-09"]},{"key":"dc:publisher","label":"Institution","values":["Virginia Tech"]},{"key":"dc:type","label":"Dc Type","values":["Thesis"]},{"key":"thesis:degree_discipline","label":"Discipline","values":["Biological Systems Engineering"]},{"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":["re-phosphorylation","dephosphorylation","energy","protein gel","casein"]}]},{"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":["etd-04222010-114302"]},{"key":"dc:identifier.uri","label":"Identifier URI","values":["http://hdl.handle.net/10919/31829"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description.abstract","label":"Abstract","values":["Nature is able to convert chemical energy into mechanical work under modest conditions, i.e., physiological pH and ambient temperature and pressure. One of the most interesting systems is muscle modeled as the \"sliding filament\" system. The sliding filament system is a combination of a thin actin filament and a thick myosin filament that slide over one another by breaking the \"energy-rich\" pyrophosphate bond of ATP. The energy from ATP hydrolysis is used for mechanical motion and the energy lost during this process is used to heat our body. In biology, the sliding filament system is taken as a fairly effective model. For engineering systems, the energy lost to heat needs to be reduced to build an efficient energy converter. In our research, we use a phosphate charged protein, casein, and react it with divinyl sulfone (DVS) through a Michael addition reaction to produce a cross-linked gel. The protein gel could be ephosphorylated at standard conditions using bovine phosphatase (bp) and re-phosporylated using casein kinase. When attached to the protein, the negatively charged phosphate groups cause the gel to expand from repulsion. When removed, the protein contracts. Therefore, work is realized without sliding friction, which is the origin of the large energy loss in muscle. FT-IR spectroscopy allows us to follow the two biochemical reactions. We also show a thermodynamic analysis of the work and offer an estimation of the most basic term."]},{"key":"dc:description.degree","label":"Dc Description Degree","values":["Master of Science"]},{"key":"dc:title","label":"Title","values":["Direct conversion of chemical energy to mechanical work using a phosphate charged protein"]}]}],"canonical_facts":{"dc:contributor.committeechair":["Barone, Justin R."],"dc:contributor.committeemember":["Senger, Ryan S.","Freeman, Joseph W."],"dc:contributor.department":["Biological Systems Engineering"],"dc:creator":["Shen, Ying"],"dc:date.accessioned":["2014-03-14T20:34:02Z"],"dc:date.available":["2014-03-14T20:34:02Z","2010-05-25"],"dc:date.issued":["2010-04-09"],"dc:description.abstract":["Nature is able to convert chemical energy into mechanical work under modest conditions, i.e., physiological pH and ambient temperature and pressure. One of the most interesting systems is muscle modeled as the \"sliding filament\" system. The sliding filament system is a combination of a thin actin filament and a thick myosin filament that slide over one another by breaking the \"energy-rich\" pyrophosphate bond of ATP. The energy from ATP hydrolysis is used for mechanical motion and the energy lost during this process is used to heat our body. In biology, the sliding filament system is taken as a fairly effective model. For engineering systems, the energy lost to heat needs to be reduced to build an efficient energy converter. In our research, we use a phosphate charged protein, casein, and react it with divinyl sulfone (DVS) through a Michael addition reaction to produce a cross-linked gel. The protein gel could be ephosphorylated at standard conditions using bovine phosphatase (bp) and re-phosporylated using casein kinase. When attached to the protein, the negatively charged phosphate groups cause the gel to expand from repulsion. When removed, the protein contracts. Therefore, work is realized without sliding friction, which is the origin of the large energy loss in muscle. FT-IR spectroscopy allows us to follow the two biochemical reactions. We also show a thermodynamic analysis of the work and offer an estimation of the most basic term."],"dc:description.degree":["Master of Science"],"dc:identifier.other":["etd-04222010-114302"],"dc:identifier.uri":["http://hdl.handle.net/10919/31829"],"dc:publisher":["Virginia Tech"],"dc:rights":["In Copyright"],"dc:rights.uri":["http://rightsstatements.org/vocab/InC/1.0/"],"dc:subject":["re-phosphorylation","dephosphorylation","energy","protein gel","casein"],"dc:title":["Direct conversion of chemical energy to mechanical work using a phosphate charged protein"],"dc:type":["Thesis"],"thesis:degree_discipline":["Biological Systems Engineering"],"thesis:degree_level":["masters"],"thesis:degree_name":["Master of Science"],"thesis:institution_name":["Virginia Polytechnic Institute and State University"]},"updated_at":"2026-07-22T22:19:32Z"}