Linked Life Data

17910025

Source:http://linkedlifedata.com/resource/pubmed/id/17910025

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
16
pubmed:dateCreated
2007-11-7
pubmed:abstractText
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.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
1439-4235
pubmed:author
pubmed:issnType
Print
pubmed:day
12
pubmed:volume
8
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
2309-13
pubmed:meshHeading
pubmed:year
2007
pubmed:articleTitle
Strategies for measurements of pseudocontact shifts in protein NMR spectroscopy.
pubmed:affiliation
Institut für Anorganische Chemie, Georg August Universität, Tammannstrasse 4, 37073 Göttingen, Germany.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't