Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1998-1-27
pubmed:abstractText
A Gill titration calorimeter is evaluated as an instrument to determine in one experiment the equilibrium constant and the enthalpy change of a biochemical reaction. The dimensionless parameter kc (the product of the association equilibrium constant and the concentration of the reagent to be titrated; Wiseman et al., Anal. Biochem. 179, 131-137, 1989) is used to analyze the instrument performance. The analysis of simulated titration data corresponding to a simple model case shows that association equilibrium constants in the 10(2)-10(7) M-1 range may be determined when the kc parameter is between 1 and 1000. In addition we use a Monte Carlo approach to estimate the precision in the thermodynamic parameters of the reaction under study. The relative precision in the calculated constants ranges from 3 to 80% depending on the macromolecule concentration and kc value in the experiment. These results were checked with the study of the reactions of beta-trypsin with its inhibitor and ribonuclease A with cytidine 2'-monophosphate and cytidine 3'-monophosphate.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0003-2697
pubmed:author
pubmed:copyrightInfo
Copyright 1997 Academic Press.
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
254
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
96-108
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:year
1997
pubmed:articleTitle
Measurement of biochemical affinities with a Gill titration calorimeter.
pubmed:affiliation
Facultad de Ciencias, Universidad de Granada, Granada, 18071, Spain.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't