The
rate of water proton relaxation of protein solutions were studied
in the presence and absence of the paramagnetic ions[gadolinium (III), manganese (II),
chromium (III), iron (III), nickel (II), copper (II), and cobalt (II)] in the previous studies. However,
these studies were carried out rather at low frequencies. Therefore, studying
of temperature dependence of relaxation rates for absence and presence of 2 %
albumin in pure D2O by 400 MHz will be a novelty.
In this study, T1 and T2 relaxation
ratios of D2O and 0.1 H2O/0.9D2O solutions were investigated with respect to
temperature for pure and for
constant albumin concentration(2%). The experiments were
carried out by using Bruker Avance 400 MHz NMR. Inversion Recovery (180-τ-90)
pulse step were used for T1, whereas Carr-Purcell-Meiboom-Gill pulse
step were used for T2. The
experiments were performed for temperature range of 20°C-40°C by using
automatic temperature control unit.
1/T1 and 1/T2
decrease linearly with increasing temperature for pure D2O
solutions. However, for 0.1H2O/0.9D2O solutions, the
relaxation rates of T1 increase with increasing temperature while T2
decreases with increasing temperature. The
decrease in both relaxation rates of the D2O solution with respect
to the increased temperature suggests that relaxation is due to spin relaxation
interaction. Increasing of relaxation rates with the increasing temperature, in
the presence of albumin demonstrates the validity of the
dipolar mechanism
Primary Language | English |
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Subjects | Metrology, Applied and Industrial Physics |
Journal Section | Article |
Authors | |
Publication Date | June 4, 2018 |
Submission Date | March 2, 2018 |
Acceptance Date | April 2, 2018 |
Published in Issue | Year 2018 Volume: 4 Issue: 1 |
This work is licensed under a Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International License.