| Improving the chemical shift dispersion of multidimensional NMR spectra of intrinsically disordered proteins. | |
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MedLine Citation:
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PMID: 23314728 Owner: NLM Status: Publisher |
Abstract/OtherAbstract:
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Intrinsically disordered proteins (IDPs) have recently attracted the attention of the scientific community challenging the well accepted structure-function paradigm. In the characterization of the dynamic features of proteins nuclear magnetic resonance spectroscopy (NMR) is a strategic tool of investigation. However the peculiar properties of IDPs, with the lack of a unique 3D structure and their high flexibility, have a strong impact on NMR observables (low chemical shift dispersion, efficient solvent exchange broadening) and thus on the quality of NMR spectra. Key aspects to be considered in the design of new NMR experiments optimized for the study of IDPs are discussed. A new experiment, based on direct detection of (13)C(α), is proposed. |
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Authors:
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Wolfgang Bermel; Marta Bruix; Isabella C Felli; Vasantha Kumar M V; Roberta Pierattelli; Soraya Serrano |
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Publication Detail:
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Type: JOURNAL ARTICLE Date: 2013-1-12 |
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: 2013-1-14 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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Bruker BioSpin GmbH, 76287, Rheinstetten, Germany. |
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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