[A study of interactions of carbonic anhydrase B with water and urea. I. Spin-diffusion parameters that determine individual and cooperative properties of molecules].
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.
Kutyshenko
V P
VP
Prokhorov
D A
DA
Khristoforov
V S
VS
D024401:Carbonic Anhydrase I / Q000737:chemistry*; D019906:Nuclear Magnetic Resonance, Biomolecular; D014508:Urea / Q000737:chemistry*; D014867:Water / Q000737:chemistry*
D014867:Water; D014508:Urea; D024401:Carbonic Anhydrase I