High-field NMR T1 and T2 relaxation mechanism in BSA solutions
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Tarih
2020
Yazarlar
Dergi Başlığı
Dergi ISSN
Cilt Başlığı
Yayıncı
Nova Science Publishers, Inc.
Erişim Hakkı
info:eu-repo/semantics/closedAccess
Özet
In this study, the proton spin-lattice and spin-spin relaxation times of BSA solutions were investigated as a function of concentration and temperature. All tests were repeated three times and the results were expressed as the average of three independent experiments. Relaxation rates were plotted versus protein concentrations. The slope of relation was taken as relaxivity. Temperature dependence of relaxation time measurements were carried out in two concentrations of BSA solutions at temperatures from 233K to 304K. The Logarithm of the spin-lattice relaxation times 71 were plotted versus inverse temperature 1/T. It was seen that NMR relaxation measurements (T1) have a dependence on the concentration and temperature of each sample. The 1/T1 relaxation rates increases as the protein concentration increases, and decreases with increasing temperature. The Bloembergen-Purcell-Pound relaxation theory were integrated with a two-state model for explaining of this data. The activation energies (Eact), and correlation times (?c ) were calculated by using the experimental data and relaxation theory related. These results were correlated well with the results from other measurements techniques. This indicates that the protein reduces the motion of water molecules and the temperature increases the motion of the water molecules. © 2020 Nova Science Publishers, Inc.
Açıklama
Anahtar Kelimeler
1tnmr, Bsa, Relaxivity, T1 And T2 Relaxation Times
Kaynak
Bovine Serum Albumin: Properties and Applications
WoS Q Değeri
Scopus Q Değeri
N/A
