Why is binding of a divalent metal cation to a structural motif containing four carboxylate residues not accompanied by a conformational change?

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Title: Why is binding of a divalent metal cation to a structural motif containing four carboxylate residues not accompanied by a conformational change?
Authors: Lushchekina S; Department of Biomolecular Sciences, Weizmann Institute of Science, Rehovot, Israel., Weiner L; Department of Brain Sciences, Weizmann Institute of Science, Rehovot, Israel.; Department of Chemical Research Support, Weizmann Institute of Science, Rehovot, Israel., Ashani Y; Department of Biomolecular Sciences, Weizmann Institute of Science, Rehovot, Israel., Emrizal R; Department of Applied Physics, Faculty of Science and Technology, Universiti Kebangsaan Malaysia, Bangi, Malaysia., Firdaus-Raih M; Department of Applied Physics, Faculty of Science and Technology, Universiti Kebangsaan Malaysia, Bangi, Malaysia.; Institute of Systems Biology, Universiti Kebangsaan Malaysia, Bangi, Malaysia., Silman I; Department of Brain Sciences, Weizmann Institute of Science, Rehovot, Israel., Sussman JL; Department of Chemical and Structural Biology, Weizmann Institute of Science, Rehovot, Israel.; Structural Proteomics Unit, Life Sciences Core Facilities, Weizmann Institute of Science, Rehovot, Israel.
Source: Protein science : a publication of the Protein Society [Protein Sci] 2024 Dec; Vol. 33 (12), pp. e5206.
Publication Type: Journal Article; Research Support, Non-U.S. Gov't
Journal Info: Publisher: Cold Spring Harbor Laboratory Press Country of Publication: United States NLM ID: 9211750 Publication Model: Print Cited Medium: Internet ISSN: 1469-896X (Electronic) Linking ISSN: 09618368 NLM ISO Abbreviation: Protein Sci Subsets: MEDLINE
Database: MEDLINE Ultimate
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  Data: Why is binding of a divalent metal cation to a structural motif containing four carboxylate residues not accompanied by a conformational change?
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  Data: <searchLink fieldCode="AU" term="%22Lushchekina+S%22">Lushchekina S</searchLink>; Department of Biomolecular Sciences, Weizmann Institute of Science, Rehovot, Israel.<br /><searchLink fieldCode="AU" term="%22Weiner+L%22">Weiner L</searchLink>; Department of Brain Sciences, Weizmann Institute of Science, Rehovot, Israel.; Department of Chemical Research Support, Weizmann Institute of Science, Rehovot, Israel.<br /><searchLink fieldCode="AU" term="%22Ashani+Y%22">Ashani Y</searchLink>; Department of Biomolecular Sciences, Weizmann Institute of Science, Rehovot, Israel.<br /><searchLink fieldCode="AU" term="%22Emrizal+R%22">Emrizal R</searchLink>; Department of Applied Physics, Faculty of Science and Technology, Universiti Kebangsaan Malaysia, Bangi, Malaysia.<br /><searchLink fieldCode="AU" term="%22Firdaus-Raih+M%22">Firdaus-Raih M</searchLink>; Department of Applied Physics, Faculty of Science and Technology, Universiti Kebangsaan Malaysia, Bangi, Malaysia.; Institute of Systems Biology, Universiti Kebangsaan Malaysia, Bangi, Malaysia.<br /><searchLink fieldCode="AU" term="%22Silman+I%22">Silman I</searchLink>; Department of Brain Sciences, Weizmann Institute of Science, Rehovot, Israel.<br /><searchLink fieldCode="AU" term="%22Sussman+JL%22">Sussman JL</searchLink>; Department of Chemical and Structural Biology, Weizmann Institute of Science, Rehovot, Israel.; Structural Proteomics Unit, Life Sciences Core Facilities, Weizmann Institute of Science, Rehovot, Israel.
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  Data: <searchLink fieldCode="JN" term="%229211750%22">Protein science : a publication of the Protein Society</searchLink> [Protein Sci] 2024 Dec; Vol. 33 (12), pp. e5206.
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              Text: 2024 Dec
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