Yilmaz, A.Zengin, B.2024-04-242024-04-2420130021-90371573-8647https://doi.org/10.1007/s10812-013-9769-5https://hdl.handle.net/11468/14686400 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.eninfo:eu-repo/semantics/closedAccessProton400 Mhz NmrHdoT-2-RelaxationSpin RotationAlbuminArticle803335340WOS:0003216423000042-s2.0-8488498453110.1007/s10812-013-9769-5Q4Q4