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Investigation of Temperature Dependence of Protein Solutions by NMR Spectroscopy

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Abstract

In this work, the proton spin–lattice (T1) and spin–spin (T2) relaxation times of aqueous solutions of bovine serum albumin (BSA) were investigated as a function of temperature. The T1 relaxation times were measured versus temperature (T) for five H2O solutions containing different BSA concentrations. The sample temperature was varied from 304 to 253 K for each concentration. T2 measurements were carried out versus the BSA concentrations only. The least-square fitting of ln(T1) versus T−1 yields a linear correlation. The effective correlation times \(\tau_{1}\) for T1 and \(\tau_{2}\) for T2 were calculated by using experimental data and the related theory. The data suggest that surface water is responsible for the dipolar relaxation mechanisms. Both T1 and T2 mechanisms are caused by overall tumbling of albumin molecule causing the rotational correlation time. However, some slow motions may contribute to the T2 mechanism.

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Acknowledgements

This research was supported by the Technological Research Council of Turkey (TÜBİTAK). Thanks to Professor Gareth Morris of Manchester University, and Professor Ali Yılmaz of Batman University for their assistance.

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  1. Department of Physics, Dicle University, Diyarbakir, Turkey

    Gülten Kavak Balcı

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Kavak Balcı, G. Investigation of Temperature Dependence of Protein Solutions by NMR Spectroscopy. J Solution Chem 50, 232–239 (2021). https://doi.org/10.1007/s10953-021-01052-z

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  • DOI: https://doi.org/10.1007/s10953-021-01052-z

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