Titration calorimetry of anesthetic-protein interaction: negative enthalpy of binding and anesthetic potency
نویسندگان
چکیده
منابع مشابه
Direct measurement of protein binding energetics by isothermal titration calorimetry.
Of all the techniques that are currently available to measure binding, isothermal titration calorimetry is the only one capable of measuring not only the magnitude of the binding affinity but also the magnitude of the two thermodynamic terms that define the binding affinity: the enthalpy (AH) and entropy (AS) changes. Recent advances in instrumentation have facilitated the development of experi...
متن کاملIsothermal titration calorimetry of protein-protein interactions.
The interaction of biologicalmacromolecules, whether protein-DNA, antibody-antigen, hormone-receptor, etc., illustrates the complexity and diversity of molecular recognition. The importance of such interactions in the immune response, signal transduction cascades, and gene expression cannot be overstated. It is of great interest to determine the nature of the forces that stabilize the interacti...
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Most of the biological phenomena are influenced by intermolecular recognition and interaction. Thus, understanding the thermodynamics of biomacromolecule ligand interaction is a very interesting area in biochemistry and biotechnology. One of the most powerful techniques to obtain precise information about the energetics of (bio) molecules binding to other biological macromolecules is isoth...
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ژورنال
عنوان ژورنال: Biophysical Journal
سال: 1997
ISSN: 0006-3495
DOI: 10.1016/s0006-3495(97)78827-1