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 an
Biomolecular interaction analysis: affinity biosensor technologies for functional analysis of proteins
β Scribed by Magnus Malmqvist; Robert Karlsson
- Book ID
- 104414956
- Publisher
- Elsevier Science
- Year
- 1997
- Tongue
- English
- Weight
- 665 KB
- Volume
- 1
- Category
- Article
- ISSN
- 1367-5931
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β¦ Synopsis
The introduction of affinity-based biosensors has permitted label-free functional analysis of biomolecular interactions in real time. A variety of methods are now based on BIACORE and IAsys technology and have mainly been used to determine kinetics and affinity constants.
π SIMILAR VOLUMES
The use of instrumental biosensors in basic research to measure biomolecular interactions in real time is increasing exponentially. Applications include proteinprotein, protein-peptide, DNA-protein, DNA-DNA, and lipid-protein interactions. Such techniques have been applied to, for example, antibody-
In biological systems, weak-affinity interactions (association constant, K a , of less than approximately 10 4 M Οͺ 1 ) between biomolecules are common and essential to the integrity of such units. However, studies of weak biological interactions are difficult due to the scarcity of analytical method