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2012 | 121 | 2 | 434-438
Article title

Molecular Dynamics in Biological Systems Observed by NMR Relaxation in a Rotating Frame

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EN
Abstracts
EN
NMR relaxation provides powerful tools for obtaining information on three-dimensional structures, dynamic properties and intermolecular interactions of biological macromolecules. One of these methods, called dispersion profile, is based on measuring the field dependence of spin-relaxation rates in the rotating frame, R_{1ρ} = 1/T_{1ρ}, in the presence of a low magnetic field B_1. In the presented study we use this method for investigation of molecular dynamics in protein samples. Dispersion profiles can be predicted theoretically and using two models, assuming either dipolar interaction between protons or power law dispersion, we have evaluated some molecular dynamic parameters of water adsorbed on protein surface. Our researches are focused on the connections of obtained parameters of molecular dynamics with conformation changes of protein. We have calculated the correlation times and power parameters for samples of lyophilized powder of albumins (egg white and bovine and rabbit blood serum) and lysozyme, as well as its aqueous solutions. Analysis of these parameters yields valuable information on the molecular nature of investigated biological systems. We also used this method to analyze experimental data of T_{1ρ} obtained by other authors for bovine serum albumin and we have found good accordance with their conclusions concerning molecular dynamics of proteins.
Keywords
EN
Year
Volume
121
Issue
2
Pages
434-438
Physical description
Dates
published
2012-02
References
  • [1] Y.A. Goddard, J.-P. Korb, R.G. Bryant, J. Magn. Reson. 199, 68 (2009)
  • [2] V.A. Jarymowycz, M.J. Stone, Chem. Rev. 106, 1624 (2006)
  • [3] C.-L. Teng, H. Hong, S. Kühne, R.G. Bryant, J. Magn. Reson. 148, 31 (2001)
  • [4] J.-P. Korb, A. Van-Quynh, R.G. Bryant, Chem. Phys. Lett. 339, 77 (2001)
  • [5] G. Schauer, R. Kimmich, W. Nusser, Biophys. J. 53, 397 (1988)
  • [6] E.L. Chen, R.J. Kim, PLoS One 5, e8565 (2010)
  • [7] B. Blicharska, H. Peemoeller, M. Witek, J. Magn. Reson. 207, 287 (2010)
  • [8] S.K. Koskinen, P.T. Niemi, S.A. Kajander, M.E.S. Komu, J. Magn. Reson. Imag. 24, 295 (2006)
  • [9] H.I. Mäkelä, O.H.J. Gröhn, M.I. Kettunen, R.A. Kauppinen, Biochem. Biophys. Res. Commun. 289, 813 (2001)
  • [10] S.K. Koskinen, H. Ylä-Outinen, H.J. Aho, M.E.S. Komu, Acta Radiol. 38, 1071 (1997)
  • [11] J.S. Blicharski, Acta Phys. Pol. A 41, 223 (1972)
  • [12] B. Blicharska, Z. Florkowski, J.W. Hennel, G. Held, F. Noack, Biochim. Biophys. Acta 207, 381 (1970)
  • [13] B. Halle, P.V. Denisov, Biophys. J. 69, 242 (1995)
Document Type
Publication order reference
YADDA identifier
bwmeta1.element.bwnjournal-article-appv121n259kz
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