Linked Life Data

17406231

Source:http://linkedlifedata.com/resource/pubmed/id/17406231

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2007-4-4
pubmed:abstractText
An important goal in drug development is to engineer inhibitors and ligands that have high binding affinities for their target molecules. In optimizing these interactions, the precise determination of the binding affinity becomes progressively difficult once it approaches and surpasses the nanomolar level. Isothermal titration calorimetry (ITC) can be used to determine the complete binding thermodynamics of a ligand down to the picomolar range by using an experimental mode called displacement titration. In a displacement titration, the association constant of a high-affinity ligand that cannot be measured directly is artificially lowered to a measurable level by premixing the protein with a weaker competitive ligand. To perform this protocol, two titrations must be carried out: a direct titration of the weak ligand to the target macromolecule and a displacement titration of the high-affinity ligand to the weak ligand-target macromolecule complex. This protocol takes approximately 5 h.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
1750-2799
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
1
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
186-91
pubmed:dateRevised
2008-3-24
pubmed:meshHeading
pubmed:year
2006
pubmed:articleTitle
Isothermal titration calorimetry to determine association constants for high-affinity ligands.
pubmed:affiliation
Institute of Biocomputation and Complex Systems Physics, Corona de Aragón 42, Zaragoza, E-50009, Spain.
pubmed:publicationType
Journal Article, Research Support, N.I.H., Extramural