High-field NMR T 2 relaxation mechanism in D2O solutions of albumin
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Tarih
2013
Yazarlar
Dergi Başlığı
Dergi ISSN
Cilt Başlığı
Yayıncı
Springer
Erişim Hakkı
info:eu-repo/semantics/closedAccess
Özet
400 MHz NMR T (2) in D2O solutions of albumin and pure D2O were measured at different temperatures. A relation, based on the chemical exchange between bound HDO and non-exchangeable protein protons, was derived theoretically for the contributions of bound HDO [P (b)(1/T (2b))]. A second relation was also derived theoretically by considering spin-rotation interactions between bound HDO and surrounding protein protons. The P (b)(1/T (2b)) values in albumin solutions were then determined by replacing experimental data into the first relation. The values of the 1/T (2) and P (b)(1/T (2b)) in albumin solutions increase linearly with temperature(T), whereas the 1/T (2) in D2O decreases with T. In addition, the spin-rotation correlation times were calculated from the second relation. The dipolar correlation time of albumin was then reproduced from the spin-rotation correlation times for confirmative purposes. In conclusion, the 1/T (2) in albumin solutions with D2O is caused by spin-rotation interactions.
Açıklama
Anahtar Kelimeler
Proton, 400 Mhz Nmr, Hdo, T-2-Relaxation, Spin Rotation, Albumin
Kaynak
Journal of Applied Spectroscopy
WoS Q Değeri
Q4
Scopus Q Değeri
Q4
Cilt
80
Sayı
3
