The Investigation of Serum Proteins By NMR Spectrometer


  • İlhan Candan Department of Physics, Dicle University, Turkey
  • Gulten Kavak Balcı Department of Physics, Dicle University, Turkey



H NMR, α, β, γ-globulins


In this study, the spin-lattice relaxation times of serum proteins α, β, and γ-globulins were measured with an FT-NMR spectrometer operating at 60 MHz. Relaxation rates measured as a function of concentration were plotted against protein concentrations. NMR spin lattice relaxation measurements (T1) were found to be concentration-dependent. Settlement rates increase as protein concentration increases. To explain these data, Bloembergen-Purcell-Pound relaxation theory was integrated with a two-state model. Correlation times (τ) were calculated using relevant experimental data and relaxation theory. The results obtained were found to be compatible with the results obtained from other measurement techniques. This shows that the protein reduces the movement of water molecules. The least squares fit of TP versus 1/T1 gives a linear relationship. The results show that NMR relaxation measurements can be used to study structure changes in protein solutions and that the T1 mechanism in solutions results from the fast chemical exchange of water molecules between protein-bound water and free water.




How to Cite

Candan, İlhan, & Balcı, G. K. (2023). The Investigation of Serum Proteins By NMR Spectrometer. AS-Proceedings, 1(7), 878–881.