| Probing non-specific interactions of Ca(2+)-calmodulin in E. coli lysate. | |
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MedLine Citation:
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PMID: 23324860 Owner: NLM Status: Publisher |
Abstract/OtherAbstract:
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The biological environment in which a protein performs its function is a crowded milieu containing millions of molecules that can potentially lead to a great many transient, non-specific interactions. NMR spectroscopy is especially well suited to study these weak molecular contacts. Here, non-specific interactions between the Ca(2+)-bound form of calmodulin (CaM) and non-cognate proteins in Escherichia coli lysate are explored using Ile, Leu, Val and Met methyl probes. Changes in CaM methyl chemical shifts as a function of added E. coli lysate are measured to determine a minimum 'average' dissociation constant for interactions between Ca(2+)-CaM and E. coli lysate proteins. (2)H R ( 2 ) and (13)C R ( 1 ) spin relaxation rates report on the binding reaction as well. Our results further highlight the power of methyl containing side-chains for characterizing biomolecular interactions, even in complex in-cell like environments. |
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Authors:
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Michael P Latham; Lewis E Kay |
Publication Detail:
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Type: JOURNAL ARTICLE Date: 2013-1-17 |
Journal Detail:
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Title: Journal of biomolecular NMR Volume: - ISSN: 1573-5001 ISO Abbreviation: J. Biomol. NMR Publication Date: 2013 Jan |
Date Detail:
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Created Date: 2013-1-17 Completed Date: - Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 9110829 Medline TA: J Biomol NMR Country: - |
Other Details:
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Languages: ENG Pagination: - Citation Subset: - |
Affiliation:
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Departments of Molecular Genetics, Biochemistry and Chemistry, The University of Toronto, Toronto, ON, M5S 1A8, Canada. |
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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