Nuclear Magnetic Resonance of Rotational Mobility of Mouse Hemoglobin Labeled with [2- ¹³ C]Histidine

Abstract

Carbon-13 nuclear magnetic resonance studies were made on mouse hemoglobin specifically labeled at the C-2 histidine position. Measurement of the spin lattice relaxation times of the label before and after hemolysis of the erythrocytes provides information on the intracellular fluid viscosities.

19F NMR Spectroscopy as a Probe of Cytoplasmic Viscosity and Weak Protein Interactions in Living Cells

“…15 N and 13 C NMR relaxation analyses are routinely used to assess protein dynamics 10 . 19 F atom longitudinal and transverse relaxation times ( T 1 and T 2 , respectively) have also been applied to quantify mobility5a, 11 and internal motion 11. Model‐free approaches,12 characterized by order parameters, S 2 , an overall tumbling correlation time, τ c , and internal correlation times, τ i , are commonly employed.…”

Observing the deoxy myoglobin and hemogobin signals from rat myocardium in situ

“…Erythrocyte Hb should not exhibit any detectable signal, implying that previously reported observation of erythrocyte Hb signals may arise from in vitro experimental artifacts [13–16]. Such a conclusion opposes the findings from numerous studies, indicating that the erythrocyte Hb signal should indeed be NMR visible and that the cellular microviscosity does not impede the Hb rotational diffusion [10, 17–22].…”

Human erythrocyte metabolism studies by 1H spin echo NMR

“…Within the last four years, NMR has been added to this list of techniques by the use of both 31P [2,3] and 13C [4] in studies of whole red cells. NMR has a unique advantage over most investigation procedures in that it allows a non-invasive inspection of even the most delicately balanced system.…”