Decay of dipolar order in diamagnetic and paramagnetic proteins and protein gels.
Magnetic relaxation in solids may be complicated by the creation and loss of dipolar order at finite rates. In tissues the molecular and spin dynamics may be significantly different because of the relatively high concentration of water. We have applied a modified Jeneer-Broekaert pulse sequence to measure dipolar relaxation rates in both dry and hydrated protein systems that may serve as magnetic models for tissue. In lyophilized and dry serum albumin, the dipolar relaxation time, T(1D) is on the order of 1 ms and is consistent with earlier reports. When hydrated by deuterium oxide, the dipolar relaxation times measured were on the order of tens of microseconds. When paramagnetic centers are included in the protein, the Jeneer-Broekaert echo decay times became the order of the decay time for transverse magnetization, i.e., the order of 10 micros or less. In the hydrated or paramagnetic systems, the dipolar relaxation times are too short to require inclusion in the quantitative analysis of magnetization transfer experiments.
Danek
A N
AN
Chemistry Department, University of Virginia, Charlottesville, Virginia, 22901, USA.
Bryant
R G
RG
D005612:Freeze Drying; D005782:Gels; D009682:Magnetic Resonance Spectroscopy; D008280:Magnetics; D008670:Metals; D011506:Proteins; D012710:Serum Albumin, Bovine
D005782:Gels; D008670:Metals; D011506:Proteins; D012710:Serum Albumin, Bovine