Abstract
The state of bound water in crystalized lysozyme was studied by four techniques: electret thermal depolarization currents, thermal-stimulated pressure, isothermal polization decay, and thermogravimetry. Hydration levels ranged from 0 to 40 mg water/g protein. Desorption of bound water dipoles was found to be the main process responsible for electrical depolarization. Two different binding sites for water were identified with long relaxation times at room temperature (order 10(2)s) and activation energies of 0.34 plus or minus 0.02 eV and 0.55 plus or minus 0.04 eV.
Full text
PDF
Selected References
These references are in PubMed. This may not be the complete list of references from this article.
- Fröhlich H. The extraordinary dielectric properties of biological materials and the action of enzymes. Proc Natl Acad Sci U S A. 1975 Nov;72(11):4211–4215. doi: 10.1073/pnas.72.11.4211. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Fung B. M. Proton and deuteron relaxation of muscle water over wide ranges of resonance frequencies. Biophys J. 1977 May;18(2):235–239. doi: 10.1016/S0006-3495(77)85610-5. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Harvey S. C., Hoekstra P. Dielectric relaxation spectra of water adsorbed on lysozyme. J Phys Chem. 1972 Oct 12;76(21):2987–2994. doi: 10.1021/j100665a011. [DOI] [PubMed] [Google Scholar]
- Hazlewood C. F. Physicochemical state of ions and water in living tissues and model systems. Ann N Y Acad Sci. 1973 Mar 30;204:1–631. [PubMed] [Google Scholar]
- Takashima S., Schwan H. P. Dielectric dispersion of crystalline powders of amino acids, peptides, and proteins. J Phys Chem. 1965 Dec;69(12):4176–4182. doi: 10.1021/j100782a019. [DOI] [PubMed] [Google Scholar]