Yazarlar

• Korunur, Sibel(1)
• Ulak, F. Sadan(1)
• Yilmaz, A.(1)
• Zengin, B.(1)

• MakaleAçık Erişim2022/r/munzur/2521
  Calculation of Dynamic Properties of Drug-Added Aqueous Solutions with T1 and T2 Relaxation Times; [İlaç Katkılı Sulu Çözeltilerin Dinamik Özelliklerinin T1 ve T2 Rölaksasyon Zamanları ile Hesaplanması]

  Korunur, Sibel

  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 MHz1H-NMR Spectrometer, and activation energies (E! ) and rotational correlation times (τ" and τ# ) have been determined for T1 and T2 relaxation times.

  İncele
• MakaleYalnız künye2014Scopus SJRQ4/r/munzur/4015
  NMR Proton Spin-Lattice Relaxation Mechanism in D2O Solutions of Albumin Determined at 400 MHz

  Yilmaz, A.; Zengin, B.; Ulak, F. Sadan

  T-1 values in pure D2O and D2O solutions of human serum albumin (HSA) were measured versus temperature. A formula was derived based on H-H interactions between the surface HDO and non-exchangeable protein protons. The formula was used to evaluate the average distance of the interactions (rav). The effective correlation times were then derived by replacing the experimental data in the formula. Short correlation times obtained for the solution with low HSA (0.02 g albumin for one ml of D2O) decreased from 53 to 29 ps, while longer times increased from 1.19 to 2.22 ns. They are of the order of a fraction of a nanosecond for the solution with high HSA (0.08 g albumin per one ml of D2O). The perfect consistency between the derived theory and experimental data indicates that the high-field 1/T-1 in D2O solutions of albumin is caused by dipolar interactions between the surface HDO and non-exchangeable protein protons. It also suggests that the effective correlation time of the surface HDO is of the order of the mean lifetime of short-lived surface water.

  AtıfWoS9·OpenAlex12

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