{"id":{"repo_id":"uiuc","oai_identifier":"oai:www.ideals.illinois.edu:2142/19410"},"canonical_url":"https://search.dev.ndltd.org/etd/uiuc/oai:www.ideals.illinois.edu:2142/19410","repository":{"repo_id":"uiuc","name":"University of Illinois - Urbana-Champaign","base_url":"https://www.ideals.illinois.edu/oai-pmh"},"display":{"title":"Hydration and activity studies of bovine skeletal muscle proteins and wheat gliadins by nuclear magnetic resonance","abstract":"\"$\\sp1$H and $\\sp{17}$O NMR studies of water and ion binding to bovine skeletal muscle proteins in solutions and suspensions were carried out as a function of concentration, pH/pD, and salt. Numerical analysis of the data was performed by nonlinear regression on an Apple-MacIntosh II microcomputer, using a thermodynamic linkage approach. The second virial coefficient, B$\\sb{\\rm o}$, of myosin $A$ and $B$ was obtained from the protein concentration dependence of the relaxation rates at high ionic strength (with 0.5 M NaCl). Myosin self-association in the form of tail-to-tail dimers was inferred from the NMR data in the absence of salt. At higher salt concentrations than 0.6 M NaCl, heptamer formation was inferred for myofibrillar proteins, whereas in the presence of 0.5 M NaCl, myosin was found to be fully dispersed as monomers. The \"\"binding\"\" of water to myosin $A$ appears to involve primarily carboxyl groups at high pH and imidazolium or ammonium groups at low pH, with hydration being minimal at the isoelectric point (5.5). The molecular dynamics of hydration water and ions bound to myosin occurred on a time scale of tens of picoseconds. The analysis of $\\sp{23}$Na NMR studies of Na$\\sp+$ binding to myofibrillar proteins reveals the presence of two types of binding sites on these proteins.\"","abstract_html":""$\\sp1$H and $\\sp{17}$O NMR studies of water and ion binding to bovine skeletal muscle proteins in solutions and suspensions were carried out as a function of concentration, pH/pD, and salt. Numerical analysis of the data was performed by nonlinear regression on an Apple-MacIntosh II microcomputer, using a thermodynamic linkage approach. The second virial coefficient, B$\\sb{\\rm o}$, of myosin $A$ and $B$ was obtained from the protein concentration dependence of the relaxation rates at high ionic strength (with 0.5 M NaCl). Myosin self-association in the form of tail-to-tail dimers was inferred from the NMR data in the absence of salt. At higher salt concentrations than 0.6 M NaCl, heptamer formation was inferred for myofibrillar proteins, whereas in the presence of 0.5 M NaCl, myosin was found to be fully dispersed as monomers. The ""binding"" of water to myosin $A$ appears to involve primarily carboxyl groups at high pH and imidazolium or ammonium groups at low pH, with hydration being minimal at the isoelectric point (5.5). The molecular dynamics of hydration water and ions bound to myosin occurred on a time scale of tens of picoseconds. The analysis of $\\sp{23}$Na NMR studies of Na$\\sp+$ binding to myofibrillar proteins reveals the presence of two types of binding sites on these proteins."","abstract_has_math":true,"creators":["Mora-Gutierrez, Adela"],"institution":"University of Illinois at Urbana-Champaign","degree_name":"Ph.D.","degree_level":"Dissertation","degree_discipline":"Food Science","degree_department":null,"school":null,"contributors":["Baianu, Ion C."],"advisors":[],"committee_chairs":[],"committee_members":[],"year":2011,"date_issued":"2011-05-07T12:06:38Z","date_published":"2011-05-07T12:06:38Z","updated_at":"2026-07-22T22:25:12Z","subjects":["Agriculture, Food Science and Technology"],"languages":["eng"],"rights":["Copyright 1989 Mora-Gutierrez, Adela"],"rights_urls":[],"identifier_entries":[{"key":"dc:identifier","label":"Identifier","values":["AAI8924905","(UMI)AAI8924905"],"render_values":[{"text":"AAI8924905","href":null,"code":true},{"text":"(UMI)AAI8924905","href":null,"code":true}]}]},"links":{"outbound_url":"http://hdl.handle.net/2142/19410","outbound_label":"Handle","outbound_source":"dc:identifier"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:contributor","label":"Contributor","values":["Baianu, Ion C."]},{"key":"dc:creator","label":"Author","values":["Mora-Gutierrez, Adela"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date","label":"Dc Date","values":["2011-05-07T12:06:38Z","10000-01-01","1989"]},{"key":"dc:type","label":"Dc Type","values":["text"]},{"key":"thesis:degree_discipline","label":"Discipline","values":["Food Science"]},{"key":"thesis:degree_level","label":"Degree Level","values":["Dissertation"]},{"key":"thesis:degree_name","label":"Degree Name","values":["Ph.D."]},{"key":"thesis:institution_name","label":"Thesis Institution Name","values":["University of Illinois at Urbana-Champaign"]}]},{"id":"subjects_keywords","label":"Subjects and Keywords","entries":[{"key":"dc:subject","label":"Dc Subject","values":["Agriculture, Food Science and Technology"]}]},{"id":"language_rights","label":"Language and Rights","entries":[{"key":"dc:language","label":"Dc Language","values":["eng"]},{"key":"dc:rights","label":"Dc Rights","values":["Copyright 1989 Mora-Gutierrez, Adela"]}]},{"id":"identifiers","label":"Identifiers","entries":[{"key":"dc:identifier","label":"Identifier","values":["AAI8924905","(UMI)AAI8924905","http://hdl.handle.net/2142/19410"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description","label":"Description","values":["\"$\\sp1$H and $\\sp{17}$O NMR studies of water and ion binding to bovine skeletal muscle proteins in solutions and suspensions were carried out as a function of concentration, pH/pD, and salt. Numerical analysis of the data was performed by nonlinear regression on an Apple-MacIntosh II microcomputer, using a thermodynamic linkage approach. The second virial coefficient, B$\\sb{\\rm o}$, of myosin $A$ and $B$ was obtained from the protein concentration dependence of the relaxation rates at high ionic strength (with 0.5 M NaCl). Myosin self-association in the form of tail-to-tail dimers was inferred from the NMR data in the absence of salt. At higher salt concentrations than 0.6 M NaCl, heptamer formation was inferred for myofibrillar proteins, whereas in the presence of 0.5 M NaCl, myosin was found to be fully dispersed as monomers. The \"\"binding\"\" of water to myosin $A$ appears to involve primarily carboxyl groups at high pH and imidazolium or ammonium groups at low pH, with hydration being minimal at the isoelectric point (5.5). The molecular dynamics of hydration water and ions bound to myosin occurred on a time scale of tens of picoseconds. The analysis of $\\sp{23}$Na NMR studies of Na$\\sp+$ binding to myofibrillar proteins reveals the presence of two types of binding sites on these proteins.\"","\"Binding of Mn$\\sp{2+}$ ions to wheat gliadins was studied by observing the paramagnetic relaxation enhancement of the \"\"bound\"\" water protons at 10 and 20 MHz; from such studies the number of charged carboxyl groups was found to be n = 7 $\\pm$ 1 at pH 3.4 and 25$\\sp\\circ$C, with a binding constant for Mn$\\sp{2+}$, K$\\sb{\\rm f}$ = 12.9 M$\\sp{-1}$. $\\sp\\tau\\sb{\\rm c}$ of water \"\"bound\"\" to Mn$\\sp{2+}$ attached to wheat gliadins in solutions was determined to be 18 ns.\"","Made available in DSpace on 2011-05-07T12:06:38Z (GMT). No. of bitstreams: 2 license.txt: 4922 bytes, checksum: 910b249b4beec47e7ab768910c8f966f (MD5) 8924905.pdf: 5498630 bytes, checksum: be6110d5efc33c71c185f20eb4960c93 (MD5) Previous issue date: 1989","Item marked as restricted to the 'UIUC Users [automated]' Group (id=2) by Howard Ding (hding2@illinois.edu) on 2011-05-07T14:36:46Z Item is restricted indefinitely.","Restriction data tranferred 2014-07-01T11:14:57-05:00 Original Data Group with Access UIUC Users [automated] Release Date: none Reason: ETDs are only available to UIUC Users without author permission","ETDs are only available to UIUC Users without author permission","U of I Only"]},{"key":"dc:title","label":"Title","values":["Hydration and activity studies of bovine skeletal muscle proteins and wheat gliadins by nuclear magnetic resonance"]}]}],"canonical_facts":{"dc:contributor":["Baianu, Ion C."],"dc:creator":["Mora-Gutierrez, Adela"],"dc:date":["2011-05-07T12:06:38Z","10000-01-01","1989"],"dc:description":["\"$\\sp1$H and $\\sp{17}$O NMR studies of water and ion binding to bovine skeletal muscle proteins in solutions and suspensions were carried out as a function of concentration, pH/pD, and salt. Numerical analysis of the data was performed by nonlinear regression on an Apple-MacIntosh II microcomputer, using a thermodynamic linkage approach. The second virial coefficient, B$\\sb{\\rm o}$, of myosin $A$ and $B$ was obtained from the protein concentration dependence of the relaxation rates at high ionic strength (with 0.5 M NaCl). Myosin self-association in the form of tail-to-tail dimers was inferred from the NMR data in the absence of salt. At higher salt concentrations than 0.6 M NaCl, heptamer formation was inferred for myofibrillar proteins, whereas in the presence of 0.5 M NaCl, myosin was found to be fully dispersed as monomers. The \"\"binding\"\" of water to myosin $A$ appears to involve primarily carboxyl groups at high pH and imidazolium or ammonium groups at low pH, with hydration being minimal at the isoelectric point (5.5). The molecular dynamics of hydration water and ions bound to myosin occurred on a time scale of tens of picoseconds. The analysis of $\\sp{23}$Na NMR studies of Na$\\sp+$ binding to myofibrillar proteins reveals the presence of two types of binding sites on these proteins.\"","\"Binding of Mn$\\sp{2+}$ ions to wheat gliadins was studied by observing the paramagnetic relaxation enhancement of the \"\"bound\"\" water protons at 10 and 20 MHz; from such studies the number of charged carboxyl groups was found to be n = 7 $\\pm$ 1 at pH 3.4 and 25$\\sp\\circ$C, with a binding constant for Mn$\\sp{2+}$, K$\\sb{\\rm f}$ = 12.9 M$\\sp{-1}$. $\\sp\\tau\\sb{\\rm c}$ of water \"\"bound\"\" to Mn$\\sp{2+}$ attached to wheat gliadins in solutions was determined to be 18 ns.\"","Made available in DSpace on 2011-05-07T12:06:38Z (GMT). No. of bitstreams: 2 license.txt: 4922 bytes, checksum: 910b249b4beec47e7ab768910c8f966f (MD5) 8924905.pdf: 5498630 bytes, checksum: be6110d5efc33c71c185f20eb4960c93 (MD5) Previous issue date: 1989","Item marked as restricted to the 'UIUC Users [automated]' Group (id=2) by Howard Ding (hding2@illinois.edu) on 2011-05-07T14:36:46Z Item is restricted indefinitely.","Restriction data tranferred 2014-07-01T11:14:57-05:00 Original Data Group with Access UIUC Users [automated] Release Date: none Reason: ETDs are only available to UIUC Users without author permission","ETDs are only available to UIUC Users without author permission","U of I Only"],"dc:identifier":["AAI8924905","(UMI)AAI8924905","http://hdl.handle.net/2142/19410"],"dc:language":["eng"],"dc:rights":["Copyright 1989 Mora-Gutierrez, Adela"],"dc:subject":["Agriculture, Food Science and Technology"],"dc:title":["Hydration and activity studies of bovine skeletal muscle proteins and wheat gliadins by nuclear magnetic resonance"],"dc:type":["text"],"thesis:degree_discipline":["Food Science"],"thesis:degree_level":["Dissertation"],"thesis:degree_name":["Ph.D."],"thesis:institution_name":["University of Illinois at Urbana-Champaign"]},"updated_at":"2026-07-22T22:25:12Z"}