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Total external reflection X-ray fluorescence analysis of protein-metal ion interactions in biological systems


This paper presents the results of an investigation into hemoglobin-based protein films that were formed on a liquid surface. X-ray standing wave measurements were performed at the ID 10 beamline of the European Synchrotron Radiation Facility (ESRF) and at the Langmuir station of the Kurchatov Synchrotron Radiation Source. It was found that the ability of the protein to bind metal ions is substantially increased due to the conformational rearrangements of protein macromolecules caused by various damaging effects. The elemental composition of protein preparations, which were isolated from children and adults with chronic metabolic diseases accompanied by endogenous intoxication, was analyzed. The results of the investigations offer evidence that an increase in the ligand-binding properties of the protein molecules, which was observed in model experiments using protein films, is a common trait and corresponds to in vivo processes accompanying metabolic disturbances in the body.

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Correspondence to N. N. Novikova.

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Original Russian Text © N.N. Novikova, M.V. Kovalchuk, E.A. Yur’eva, O.V. Konovalov, A.V. Rogachev, N.D. Stepina, V.S. Sukhorukov, A.D. Tsaregorodtsev, E.S. Chukhrai, S.N. Yakunin, 2012, published in Kristallografiya, 2012, Vol. 57, No. 5, pp. 727–734.

On the 100th anniversary of the discovery of X-ray diffraction

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Novikova, N.N., Kovalchuk, M.V., Yur’eva, E.A. et al. Total external reflection X-ray fluorescence analysis of protein-metal ion interactions in biological systems. Crystallogr. Rep. 57, 648–655 (2012).

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  • Crystallography Report
  • Protein Film
  • European Synchrotron Radiation Facility
  • Octadecylamine
  • Ligand Binding Property