{"@context":{"@vocab":"https://cir.nii.ac.jp/schema/1.0/","rdfs":"http://www.w3.org/2000/01/rdf-schema#","dc":"http://purl.org/dc/elements/1.1/","dcterms":"http://purl.org/dc/terms/","foaf":"http://xmlns.com/foaf/0.1/","prism":"http://prismstandard.org/namespaces/basic/2.0/","cinii":"http://ci.nii.ac.jp/ns/1.0/","datacite":"https://schema.datacite.org/meta/kernel-4/","ndl":"http://ndl.go.jp/dcndl/terms/","jpcoar":"https://github.com/JPCOAR/schema/blob/master/2.0/"},"@id":"https://cir.nii.ac.jp/crid/1363388844905526784.json","@type":"Article","productIdentifier":[{"identifier":{"@type":"DOI","@value":"10.1073/pnas.041614298"}},{"identifier":{"@type":"URI","@value":"https://pnas.org/doi/pdf/10.1073/pnas.041614298"}}],"dc:title":[{"@value":"The role of structure, energy landscape, dynamics, and allostery in the enzymatic function of myoglobin"}],"description":[{"type":"abstract","notation":[{"@value":"<jats:p>\n            The grail of protein science is the connection between structure\n and function. For myoglobin (Mb) this goal is close. Described as only\n a passive dioxygen storage protein in texts, we argue here that Mb is\n actually an allosteric enzyme that can catalyze reactions among small\n molecules. Studies of the structural, spectroscopic, and kinetic\n properties of Mb lead to a model that relates structure, energy\n landscape, dynamics, and function. Mb functions as a miniature chemical\n reactor, concentrating and orienting diatomic molecules such as NO, CO,\n O\n            <jats:sub>2</jats:sub>\n            , and H\n            <jats:sub>2</jats:sub>\n            O\n            <jats:sub>2</jats:sub>\n            in highly conserved\n internal cavities. Reactions can be controlled because Mb exists in\n distinct taxonomic substates with different catalytic properties and\n connectivities of internal cavities.\n          </jats:p>"}]}],"creator":[{"@id":"https://cir.nii.ac.jp/crid/1380294722607562752","@type":"Researcher","foaf:name":[{"@value":"Hans Frauenfelder"}],"jpcoar:affiliationName":[{"@value":"Center for Nonlinear Studies, MS-B 258, Los Alamos National\r Laboratory, Los Alamos, NM 87545; Departments of Physics\r and Chemistry, Princeton University, Princeton, NJ\r 08544; and Department of Physics, Cook Building,\r University of Vermont, Burlington, VT 05405"}]},{"@id":"https://cir.nii.ac.jp/crid/1380294722607562754","@type":"Researcher","foaf:name":[{"@value":"Benjamin H. McMahon"}],"jpcoar:affiliationName":[{"@value":"Center for Nonlinear Studies, MS-B 258, Los Alamos National\r Laboratory, Los Alamos, NM 87545; Departments of Physics\r and Chemistry, Princeton University, Princeton, NJ\r 08544; and Department of Physics, Cook Building,\r University of Vermont, Burlington, VT 05405"}]},{"@id":"https://cir.nii.ac.jp/crid/1380294722607562753","@type":"Researcher","foaf:name":[{"@value":"Robert H. Austin"}],"jpcoar:affiliationName":[{"@value":"Center for Nonlinear Studies, MS-B 258, Los Alamos National\r Laboratory, Los Alamos, NM 87545; Departments of Physics\r and Chemistry, Princeton University, Princeton, NJ\r 08544; and Department of Physics, Cook Building,\r University of Vermont, Burlington, VT 05405"}]},{"@id":"https://cir.nii.ac.jp/crid/1380294722607562755","@type":"Researcher","foaf:name":[{"@value":"Kelvin Chu"}],"jpcoar:affiliationName":[{"@value":"Center for Nonlinear Studies, MS-B 258, Los Alamos National\r Laboratory, Los Alamos, NM 87545; Departments of Physics\r and Chemistry, Princeton University, Princeton, NJ\r 08544; and Department of Physics, Cook Building,\r University of Vermont, Burlington, VT 05405"}]},{"@id":"https://cir.nii.ac.jp/crid/1380294722607562756","@type":"Researcher","foaf:name":[{"@value":"John T. Groves"}],"jpcoar:affiliationName":[{"@value":"Center for Nonlinear Studies, MS-B 258, Los Alamos National\r Laboratory, Los Alamos, NM 87545; Departments of Physics\r and Chemistry, Princeton University, Princeton, NJ\r 08544; and Department of Physics, Cook Building,\r University of Vermont, Burlington, VT 05405"}]}],"publication":{"publicationIdentifier":[{"@type":"PISSN","@value":"00278424"},{"@type":"EISSN","@value":"10916490"}],"prism:publicationName":[{"@value":"Proceedings of the National Academy of Sciences"}],"dc:publisher":[{"@value":"Proceedings of the National Academy of Sciences"}],"prism:publicationDate":"2001-02-20","prism:volume":"98","prism:number":"5","prism:startingPage":"2370","prism:endingPage":"2374"},"reviewed":"false","url":[{"@id":"https://pnas.org/doi/pdf/10.1073/pnas.041614298"}],"createdAt":"2002-07-26","modifiedAt":"2022-04-12","relatedProduct":[{"@id":"https://cir.nii.ac.jp/crid/1360861704763824384","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@value":"Genetic Perturbation Alters Functional Substates in Alkaline Phosphatase"}]},{"@id":"https://cir.nii.ac.jp/crid/1360861704778632704","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@value":"Atomic resolution protein allostery from the multi-state structure of a PDZ domain"}]},{"@id":"https://cir.nii.ac.jp/crid/2051714792003842688","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@value":"Enhanced conformational fluctuations during protein reactions"}]}],"dataSourceIdentifier":[{"@type":"CROSSREF","@value":"10.1073/pnas.041614298"},{"@type":"CROSSREF","@value":"10.1021/jacs.2c06693_references_DOI_P6WfF3GgFOQZeMyQZqCwgDU1JV9"},{"@type":"CROSSREF","@value":"10.1038/s41467-022-33687-x_references_DOI_P6WfF3GgFOQZeMyQZqCwgDU1JV9"},{"@type":"CROSSREF","@value":"10.1246/cl.190195_references_DOI_P6WfF3GgFOQZeMyQZqCwgDU1JV9"}]}