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Improving the chemical shift dispersion of multidimensional NMR spectra of intrinsically disordered proteins.
MedLine Citation:
PMID:  23314728     Owner:  NLM     Status:  Publisher    
Abstract/OtherAbstract:
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.
Authors:
Wolfgang Bermel; Marta Bruix; Isabella C Felli; Vasantha Kumar M V; Roberta Pierattelli; Soraya Serrano
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Publication Detail:
Type:  JOURNAL ARTICLE     Date:  2013-1-12
Journal Detail:
Title:  Journal of biomolecular NMR     Volume:  -     ISSN:  1573-5001     ISO Abbreviation:  J. Biomol. NMR     Publication Date:  2013 Jan 
Date Detail:
Created Date:  2013-1-14     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  9110829     Medline TA:  J Biomol NMR     Country:  -    
Other Details:
Languages:  ENG     Pagination:  -     Citation Subset:  -    
Affiliation:
Bruker BioSpin GmbH, 76287, Rheinstetten, Germany.
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