Is liquid water's relaxation rate strongly dependent on temperature, and does anyone have a link to a good online article with the dependency equation?Thanks!
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Measuring (1)H (N) temperature coefficients in invisible protein states by relaxation dispersion NMR spectroscopy.
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Abstract A method based on the Carr-Purcell-Meiboom-Gill relaxation dispersion experiment is presented for measuring the temperature coefficients of amide proton chemical shifts of low populated â??invisibleâ?? protein states that exchange with a â??visibleâ?? ground state on the millisecond time-scale. The utility of the approach is demonstrated with an application to an I58D mutant of the Pfl6 Cro protein that undergoes exchange between the native, folded state and a cold...
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Temperature dependence of fast carbonyl backbone dynamics in chicken villin headpiece subdomain
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Abstract Temperature-dependence of protein dynamics can provide information on details of the free energy landscape by probing the characteristics of the potential responsible for the fluctuations. We have investigated the temperature-dependence of picosecond to nanosecond backbone dynamics at carbonyl carbon sites in chicken villin headpiece subdomain protein using a combination of three NMR relaxation rates: 13Câ?² longitudinal rate, and two cross-correlated rates involving dipolar and...
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[NMR paper] Temperature dependence of protein backbone motion from carbonyl 13C and amide 15N NMR
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The NMR spin-lattice relaxation rate (R1) and the rotating-frame spin-lattice relaxation rate (R1rho) of amide 15N and carbonyl 13C (13C') of the uniformly 13C- and 15N-labeled ubiquitin were measured at different temperatures and field strengths to investigate the...
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The helical subdomain, HP36, of the F-actin-binding headpiece domain of chicken villin, is the smallest naturally occurring polypeptide that folds to a thermostable compact structure. Unconstrained molecular dynamics simulations and constrained molecular dynamics simulations using umbrella sampling are used to study the...
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[NMR paper] Temperature-dependence of protein hydrogen bond properties as studied by high-resolut
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The temperature-dependence of a large number of NMR parameters describing hydrogen bond properties in the protein ubiquitin was followed over a range from 5 to 65 degrees C. The parameters comprise hydrogen bond (H-bond) scalar couplings, h3JNC', chemical shifts, amide...
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Accumulation of ferritin, the iron storage protein, has been linked recently to aging and a number of pathologies. Noninvasive detection of iron storage by MRI relies on its extremely strong effect on water relaxation. The aim of this article is to characterize the effect of ferritin on transverse...
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[NMR paper] NMR relaxation data of water proton in normal tissues.
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Physiol Chem Phys Med NMR. 1996;28(4):205-38
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The spin lattice relaxation time (T1) and spin spin relaxation time (T2) of water protons of normal human and animal tissues are archived to up-date those already published. The mechanisms for water proton relaxation times of tissues are reviewed with reference to water content, paramagnetic ion, protein dynamics content and organ weight.
bulk water relaxation dependence on temperature
Linear Mode
