The longitudinal proton magnetic relaxation times TI were measured for ferri (met)and carbonmonoxy-bovine haemoglobin and equine myoglobin in 0.1 M KH2P04 aqueous solutions near pH 6 a t 5Β°C and 35Β°C from 1.5-to 60-MHx Larmor frequencies. I t is concluded that the correlation time T C for the dipole
The contribution of proton fluctuation to dielectric relaxation in protein solutions
β Scribed by G. P. South; E. H. Grant
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 1973
- Tongue
- English
- Weight
- 415 KB
- Volume
- 12
- Category
- Article
- ISSN
- 0006-3525
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β¦ Synopsis
Abstract
Equations are derived which account for the effect of an applied electric field on the fluctuation of protons associated with a macromolecule. The contribution of this proton polarization to the complex permittivity of the macromolecules is evaluated in terms of its effect on both the dispersion due to proton fluctuation and the dispersion caused by dipolar rotation. An expression for the fluctuation correlation time Ο__i__Ξ΄ is derived in terms of the mean lifetimes of the ionised and unionised state Ο0 and Ο+. If Ο__i__Ξ΄ is very much less than the dipolar correlation time Ο__i__, the fluctuation dispersion will occur at much higher frequencies than the dispersion due to orientation polarization; hence the dispersions will be well separated. If Ο__i__Ξ΄ Β» Ο__i__ the two regions would overlap and would be indistinguishable as separate entities. At present insufficient data are available to test rigorously these conclusions but the potentialities of the theory in relation to small globular proteins is shown.
π SIMILAR VOLUMES
A boundary element formulation of continuum electrostatics is used to examine time-independent dielectric relaxation and screening in two proteins, and time-dependent relaxation in two simpler solutes. Cytochrome c oxidation is modeled by inserting partial charges on the heme, using one to three die
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