Abstract
The development of modern spectroscopic methods has facilitated and accelerated structure analysis. The NMR method is the most popular way to perform structural analysis of compounds with very complex structures.D2O is a solvent that is frequently used in NMR analysis of both chemical molecules and many biological molecules such as drugs, proteins, and enzymes. In this paper, the study of residual water in proton drug-added protein solutions was carried out via NMR relaxation. The spin-lattice (T1) and the spin-spin relaxation (T2) times of residual water in drug-added protein solutions were studied depending on temperature by Avance Bruker 400 MHz 1H-NMR Spectrometer, and activation energies (Ea) and rotational correlation times (τ0 and τc) have been determined for T1 and T2 relaxation times.
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