Related Experiment Video
Updated: Aug 16, 2026

Fat-Water Phantoms for Magnetic Resonance Imaging Validation: A Flexible and Scalable Protocol
Published on: September 7, 2018
Protein-water interaction studied by solvent 1H, 2H, and 17O magnetic relaxation
Abstract:
Previous studies of the magnetic field dependence of the magnetic relaxation rate of solvent protons in protein solutions have indicated that this dependence (called relaxation dispersion) is related to the rotational Brownian motion of the solute proteins. In particular, the dispersion of the longitudinal (spin-lattice) relaxation rate 1/T1 shows a monotonic decrease with increasing field, with an inflection point corresponding to a proton Larmor frequency which is inversely proportional to the orientational relaxation time of the protein. We have now compared the relaxation dispersion of solvent 1H, 2H, and 17O In aqueous solutions of lysozyme (molecular weight 14,700) and 1H and 2H in solutions of hemocyanin (molecular weight 14,7 00) and 1H and 2H in solutions of hemocyanin (molecular weight 9 x 10(6)). The main experimental observation is that the dispersion of the relaxation rates of the three solvent nuclei in lysozyme solutions, normalized to their respective rates in pure water, is essentially the same. This is also true for 1H and 2H relaxation in hemocyanin solutions. These results confirm that entire solvent water molecules, rather than exchanging protons, are involved in the interaction. We have been unable to deduce the correct mechanism to explain the data, but we can eliminate several interaction mechanisms from consideration. For example, all observations combined cannot be explained by a simple two-site model of exchange, in which water molecules are either in sites on the protein with a relaxation rate characteristic of these sites, or else in the bulk solvent (the observed relaxation rate being the weighted average of the two). Also eliminated is the class of models in which the protein molecules induce a preferential partial alignment of neighboring solvent molecules, for example by electrostatic interaction of the electric dipole moments of the water with the electric fields produced by surface charges of the protein molecules. In addition, the idea that relaxation of solvent nuclei is due, in the main, to interactions with protein protons is precluded. Rather, it appears that the protein molecules influence the dynamics of the motion of solvent water molecules in their neighborhood in a manner that imposes on all the solvent molecules a correlation time for their orientational relaxation which equals that of the solute proteins.
Related Concept Videos
¹H NMR: Interpreting Distorted and Overlapping Signals
As Δν decreases and the signals move closer, the doublets appear increasingly distorted. The intensities of the inner lines increase at the cost of those of the outer lines as the signals are slanted or...
¹H NMR of Conformationally Flexible Molecules: Temporal Resolution
¹H NMR of Labile Protons: Temporal Resolution
The –OH proton in alcohols typically appears in the range of δ 2 to 5 ppm but can vary depending on the specific...
¹H NMR of Labile Protons: Deuterium (²H) Substitution
¹H NMR of Conformationally Flexible Molecules: Variable-Temperature NMR
Atomic Nuclei: Types of Nuclear Relaxation
In spin–lattice or longitudinal relaxation, the excited spins exchange energy with the surrounding lattice as they return to the lower energy level. Among several mechanisms that contribute to spin–lattice relaxation, magnetic dipolar interactions are significant. Here, the excited nucleus transfers energy to a nearby...
![Measuring the Spin-Lattice Relaxation Magnetic Field Dependence of Hyperpolarized [1-13C]pyruvate](/_next/image?url=https%3A%2F%2Fcloudfront.jove.com%2FCDNSource%2Fteasers%2F59399.jpg&w=3840&q=50)
