Paramagnetic relaxation of protons in rotationally immobilized proteins

The Journal of Chemical Physics
Jean-Pierre KorbR G Bryant

Abstract

The proton magnetic relaxation dispersion profiles are reported over the proton Larmor frequency range from 0.01 to 30 MHz for cross-linked gels and for the dry lyophilized bovine serum albumin covalently labeled at lysine with diethylenetriaminepentaacetic acid chelates of either Gd(III) or Mn(II) ions. The proton spin-lattice relaxation dispersion for the cross-linked paramagnetic protein gel is accurately represented as a sum of two major relaxation contributions. The diamagnetic term is a power law from the magnetic field dependence of the protein protons. The paramagnetic term is approximately described by the Solomon-Bloembergen-Morgan class of models. However, the paramagnetic relaxation mechanism in the dry lyophilized protein is fundamentally different and we develop a new quantitative description of the dispersion profile. In the dry case, no peak in the proton relaxation dispersion profile is detected from the field dependence of the electron spin relaxation times. The high-field paramagnetic relaxation dispersion is a power law in the Larmor frequency with an exponent of -0.8, which results from modulation of the electron-nuclear coupling by the intramolecular dynamics of the protein which primarily propagates along...Continue Reading

References

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Citations

Sep 29, 2011·Journal of Magnetic Resonance·A E Sitnitsky
Dec 11, 2007·Journal of Magnetic Resonance·Richard L MaginXiaohong Joe Zhou
Mar 6, 2007·Journal of Magnetic Resonance·Jean-Pierre KorbRobert G Bryant
Dec 7, 2011·Magnetic Resonance in Medicine : Official Journal of the Society of Magnetic Resonance in Medicine·Galina DiakovaRobert G Bryant
Jan 14, 2009·Magnetic Resonance in Chemistry : MRC·Hiroyuki HayashiNoboru Koga
Apr 7, 2010·Physical Review. E, Statistical, Nonlinear, and Soft Matter Physics·J-P KorbP Ligneul

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