Protonation linked equilibria and apparent affinity constants: the thermodynamic profile of the α-chymotrypsin–proflavin interaction
Author:
Publisher
Springer Science and Business Media LLC
Subject
General Medicine,Biophysics
Link
http://link.springer.com/content/pdf/10.1007/s00249-007-0148-0.pdf
Reference43 articles.
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3. Bachovchin WW (2001) Contributions of NMR spectroscopy to the study of hydrogen bonds in serine protease active sites. Magn Reson Chem 39:S199–S213
4. Baker BM, Murphy KP (1996) Evaluation of linked protonation effects in protein binding reactions using isothermal titration calorimetry. Biophys J 71:2049–2055
5. Baker BM, Murphy KP (1997) Dissecting the energetics of a protein–protein interaction: the binding of ovomucoid third domain to elastase. J Mol Biol 268:557–569
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