Hydration water, charge transport and protein dynamics
- PMID: 23345745
- PMCID: PMC3456585
- DOI: 10.1023/A:1013147430930
Hydration water, charge transport and protein dynamics
Abstract
The hydration water of proteins is essential to biological activity but its properties are not yet fully understood. A recent study of dielectric relaxation of hydrated proteins [A. Levstik et al., Phys. Rev E.60 7604 (1999)] has found a behavior typical of a proton glass, with a glass transition of about 268 K. In order to analyze these results, we investigate the statistical mechanics and dynamics of a model of `two-dimensional water' which describes the hydrogen bonding scheme of bounded water molecules. We discuss the connection between the dynamics of bound water and charge transport on the protein surface as observed in the dielectric measurements.
References
-
- Sartor G., Hallbrucker A., Hofer K., Mayer E. Calorimetric Glass-Liquid Transition and Crystallization Behavior of a Vitreous, but Freezable, Water Fraction of Hydrated Methemoglobin. J. Phys. Chem. 1992;96:5133–5138.
-
- Rupley J., Careri G. Protein Hydration and Function. Adv. Prot. Chem. 1991;41:37–172. - PubMed
-
- Reinisch L., Kaiser R.D., Krim J. Measurement of Protein Hydration Shells using a Quartz Microbalance. Phys. Rev. Lett. 1989;63:1743–1746. - PubMed
-
- Careri G., Consolini G., Bruni F. Dielectric Relaxation of a Proton Glass in Hydrated Protein Powders. Solid State Ionics. 1999;125:257–261.
LinkOut - more resources
Full Text Sources