Spin-lattice relaxation of water protons in serum adhesion protein (SAP) solutions of ultra low concentrations
β Scribed by T.A. Babushkina; T.P. Klimova; I.A. Yamskov; V.P. Yamskova
- Book ID
- 103835705
- Publisher
- Elsevier Science
- Year
- 2005
- Tongue
- English
- Weight
- 85 KB
- Volume
- 122
- Category
- Article
- ISSN
- 0167-7322
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β¦ Synopsis
Spin-lattice relaxation of water protons in serum adhesion protein (SAP) solutions of ultra low concentrations (10 Γ 13 , 10 Γ 15 , 10 Γ 16 , 10 Γ 17 , 10 Γ 19 M) are investigated in the temperature range 288 -330 K. It is shown that the Arrenius equation with two activation energies describes the experimental function T 1 = f(T). The activation energies of water proton motion for all studied solutions and for clean water have close values in the temperature range of 305 -330 K. But the activation energies of the water proton motion for SAP solutions with concentrations 10 Γ 13 , 10 Γ 15 , 10 Γ 16 , 10 Γ 19 M in the temperature range of 288 -303 K are very different from those for clean water. We suppose that a new structure of H-bond net induced by the influence of SAP can be the cause of the difference between the activation energies.
π SIMILAR VOLUMES
1H NMR spin-lattice relaxation times (T1) of the N-CH3 proton resonances of phosphocreatine (PCr) and creatine (Cr) in water solutions were obtained using the 1,3,3,1 pulse sequence. These T1 values were equivalent to those obtained in D2O and water using either the conventional inversion-recovery e