Linked Life Data

17964929

Source:http://linkedlifedata.com/resource/pubmed/id/17964929

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
2007-10-29
pubmed:abstractText
Isothermal titration calorimetry (ITC) is now routinely used to directly characterize the thermodynamics of biopolymer binding interactions and the kinetics of enzyme-catalyzed reactions. This is the result of improvements in ITC instrumentation and data analysis software. Modern ITC instruments make it possible to measure heat effects as small as 0.1 microcal (0.4 microJ), allowing the determination of binding constants, K's, as large as 10(8) - 10(9)M(-1). Modern ITC instruments make it possible to measure heat rates as small as 0.1 microcal/sec, allowing for the precise determination of reaction rates in the range of 10(-12) mol/sec. Values for K(m) and k(cat), in the ranges of 10(-2) - 10(3) microM and 0.05 - 500 sec(-1), respectively, can be determined by ITC. This chapter reviews the planning of an optimal ITC experiment for either a binding or kinetic study, guides the reader through simulated sample experiments, and reviews analysis of the data and the interpretation of the results.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0091-679X
pubmed:author
pubmed:issnType
Print
pubmed:volume
84
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
79-113
pubmed:meshHeading
pubmed:year
2008
pubmed:articleTitle
Isothermal titration calorimetry: experimental design, data analysis, and probing macromolecule/ligand binding and kinetic interactions.
pubmed:affiliation
Department of Chemistry and Biochemistry, Northern Arizona University, Flagstaff, Arizona 86011, USA.
pubmed:publicationType
Journal Article, Review, Research Support, Non-U.S. Gov't