NMR Proton Spin-Lattice Relaxation Mechanism in D2O Solutions of Albumin Determined at 400 MHz
[ X ]
Tarih
2014
Yazarlar
Dergi Başlığı
Dergi ISSN
Cilt Başlığı
Yayıncı
Springer
Erişim Hakkı
info:eu-repo/semantics/closedAccess
Özet
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.
Açıklama
Anahtar Kelimeler
Proton Nmr, Surface Hdo, Albumin
Kaynak
Journal of Applied Spectroscopy
WoS Q Değeri
Q4
Scopus Q Değeri
Q4
Cilt
81
Sayı
3
