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Investigation of the molecular mobility of peptin macromolecules using photon-correlation spectroscopy

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Abstract

The pH dependence of the intermolecular interaction coefficient of pepsin in an aqueous solution is obtained by using photon-correlation spectroscopy. The dependence shows a minimum near the isoelectric point (pH 1.6). The dynamic parameters of pepsin macromolecules in solutions containing various metal ions, including potassium, cobalt, lead, cesium, and rubidium are studied. It is shown that the addition of these ions causes a decrease of the translational diffusion coefficients. It is found that an increase in temperature leads to the structural transition of a pure solution of pepsin in water. The activation energy of this transition is calculated using the Arrhenius law.

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Authors and Affiliations

  1. Faculty of Physics, Moscow State University, Moscow, 119991, Russia

    Xiaolei Zhang, G. P. Petrova, Yu. M. Petrusevich & I. A. Sergeeva

Authors
  1. Xiaolei Zhang
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  2. G. P. Petrova
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  3. Yu. M. Petrusevich
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  4. I. A. Sergeeva
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Corresponding author

Correspondence to Xiaolei Zhang.

Additional information

Original Russian Text © Zhang Xiaolei, G.P. Petrova, Yu.M. Petrusevich, I.A. Sergeeva, 2012, published in Vestnik Moskovskogo Universiteta. Fizika, 2012, No. 1, pp. 73–77.

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Zhang, X., Petrova, G.P., Petrusevich, Y.M. et al. Investigation of the molecular mobility of peptin macromolecules using photon-correlation spectroscopy. Moscow Univ. Phys. 67, 66–70 (2012). https://doi.org/10.3103/S0027134912010201

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  • DOI: https://doi.org/10.3103/S0027134912010201

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