Investigation of the hydration of bovine serum albumin by an NMR titration method

Gulten Kavak, Ali Yilmaz, Gareth Morris, Frank Heatley

Research output: Contribution to journalArticlepeer-review


In this study, NMR titration method was used to determine the dynamics of hydration water. Solutions were made by dehydration procedures and relaxation measurements were carried out on a Vnmr (Varian NMR) spectrometer operating at 300 MHz for proton and relaxation rates (1/T1) were plotted versus Ms/Mw. It was seen that the NMR titration data was separated into 2 line segments. The intercepts of the first line segment with lower mass of solute/mass of water (Ms/Mw) ratio and the second line segment with higher Ms/Mw are 2.15 and 2.57, respectively. The correlation times for free and structured water were obtained as 5.56 × 10-12 s and 1.5 × 10-11 s, respectively. The 1/T1 and 1/T2 relaxation rates increase as the protein concentration increases. This implies that the protein is reducing the motion of water molecules. The correlation times (τc) were calculated by using the experimental data and relaxation theory related. These results suggest that the relaxation times of water layers surrounding a protein could be determined by T1 measured versus Mp/Mw. Present results were correlated well with the results from other measurements techniques. The data also suggest that the relaxation mechanism of bovine serum albumin (or serum proteins) can be explained in terms of fast chemical exchange of protons between bulk water and water bound to proteins.

Original languageEnglish
Pages (from-to)1355-1359
Number of pages5
JournalAsian Journal of Chemistry
Issue number2
Publication statusPublished - Feb 2010


  • Bovine serum albumin
  • Correlation
  • Relaxation times


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