Document Detail


Strategies for measurements of pseudocontact shifts in protein NMR spectroscopy.
MedLine Citation:
PMID:  17910025     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Paramagnetic metal ions bound to proteins generate a dipolar field that can be accurately probed by pseudocontact shifts (PCS) displayed by the protein's nuclear spins. PCS are highly useful for determining the coordinates of individual spins in the molecule and for rapid structure determinations of entire protein-protein and protein-ligand complexes. However, PCS measurements require reliable resonance assignments for the molecule in its paramagnetic state and in a diamagnetic reference state. This article discusses different approaches for pairwise resonance assignments, with emphasis on a strategy which exploits chemical exchange between the two states.
Authors:
Michael John; Gottfried Otting
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Chemphyschem : a European journal of chemical physics and physical chemistry     Volume:  8     ISSN:  1439-4235     ISO Abbreviation:  Chemphyschem     Publication Date:  2007 Nov 
Date Detail:
Created Date:  2007-11-07     Completed Date:  2007-12-11     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  100954211     Medline TA:  Chemphyschem     Country:  Germany    
Other Details:
Languages:  eng     Pagination:  2309-13     Citation Subset:  IM    
Affiliation:
Institut für Anorganische Chemie, Georg August Universität, Tammannstrasse 4, 37073 Göttingen, Germany.
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MeSH Terms
Descriptor/Qualifier:
Metalloproteins / chemistry*
Models, Molecular
Nuclear Magnetic Resonance, Biomolecular / methods*
Proteins / chemistry*
Chemical
Reg. No./Substance:
0/Metalloproteins; 0/Proteins

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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