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Hot Biological Catalysis: Isothermal Titration Calorimetry to Characterize Enzymatic Reactions
Published on: April 4, 2014
[A study of interactions of carbonic anhydrase B with water and urea. I. Spin-diffusion parameters that determine
Abstract:
The rigidity parameter (G), which is characteristic of protein compactness, was studied in native globular carbonic anhydrase B. The dependence of parameter G on power and excitation time of spin-diffusion was expressed analytically. We found out that native carbonic anhydrase B is able to form water-protein units that are probabilistically distributed with respect to their sizes. Large water-protein units can be detected by analyzing the spin-diffusion spectra. The excitation frequencies of spin-diffusion spectra were shifted far away from typical 1H NMR spectra of carbonic anhydrase B.
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