ISSN:
0952-3499
Keywords:
Kinetics
;
thermodynamics
;
protein
;
enthalpy
;
entropy
;
equilibrium
;
transition state
;
BIACORE
;
Chemistry
;
Biochemistry and Biotechnology
Source:
Wiley InterScience Backfile Collection 1832-2000
Topics:
Medicine
Notes:
A methodology using biosensor technology for combined kinetic and thermodynamic analysis of biomolecular interactions is described. Rate and affinity constants are determined with BIAcore. Thermodynamics parameters, changes in free energy, enthalpy and entropy, are evaluated from equilibrium data and by using rate constants and transition state theory. The methodology using van't Hoff theory gives complementary information to microcalorimetry, since only the direct binding is measured with BIAcore whereas microcalorimetry measures all components, including e.g. hydration effects. Furthermore, BIAcore gives possibilities to gain new information by thermodynamic analysis of the rate constants. Copyright © 1998 John Wiley & Sons, Ltd.
Additional Material:
7 Ill.
Type of Medium:
Electronic Resource
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