Abstract
The structure of complexes of various alkylhydroxybenzenes, such as 4-hexylresorcinol, 5-methyl-resorcinol, and tyrosol, is studied using experimental and theoretical methods. The influence of 4-hexyl-resorcinol and 5-methylresorcinol in a wide range of concentrations on the structure, equilibrium fluctuations, and functional activity of a water-soluble enzyme lysozyme is examined. A spatial model for the interaction of ligands and clusters thereof with the protein and the aqueous medium is constructed. A possible mechanism of the stabilization of the protein tertiary structure by the aforementioned molecules is proposed.
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W. J. Welch and C. R. Brown, Cell Stress Chaperones 1, 109 (1996).
J. Tatzelt, S. B. Prusiner, and W. J. Welch, EMBO J. 15, 6363 (1996).
A. V. Finkelstein and O. B. Ptitsyn, Protein Physics, Course of Lectures, 2nd ed. (Universitet, Moscow, 2002), p. 374 [in Russian].
A. Smith, Nature 426(6968), 883 (2003).
C. M. Dobson, Nature 426(6968), 884 (2003).
F. E. Cohen and J. W. Kelly, Nature 426, 905 (2003).
J. P. Morello, U. E. Petajea-Repo, D. G. Bichet, and M. Bouvier, TIPS 21, 466 (2000).
A. Kozubek and J. H. P. Tyman, Chem. Rev. 99, 1 (1999).
PubChem, Data Base of Biologic Activity of Small Molecules. http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi?cid=10436/
G. I. El-Registan, A. L. Mulyukin, Yu. A. Nikolaev, et al., Microbiology 75, 380 (2006).
Yu. F. Krupyanskii, E. G. Abdulnasyrov, N. G. Loiko, et al., Russ. J. Phys. Chem. B 31, 301 (2012).
Yu. F. Krupyanskii, P. P. Noks, N. G. Loiko, et al., Biophysics 56, 8 (2011).
K. B. Tereshkina and Yu. F. Krupyanskii, in Proceedings of the 20th Conference on Mathematics. Computer. Education (OIYaI, Dubna, 2013), p. 37.
A. I. Kolpakov, O. N. Il’inskaya, M. M. Bespalov, et al., Microbiology 69, 180 (2000).
I. Yu. Stepanenko, M. L. Shishkina, E. I. Martirosova, et al., in Proceedings the All-Russia Scientific-Technical Conference and Exhibition on High Effective Food Technologies, Methods and Means of their Realization (MGUPP, Moscow, 2003), p. 195.
Yu. A. Nikolaev, N. G. Loiko, I. Yu. Stepanenko, et al., Prikl. Biokhim. Mikrobiol. 44(2), 159 (2008).
Yu. F. Krupyanskii, G. V. Eshchenko, S. V. Esin, et al., Biophysics 50, 865 (2005).
Yu. F. Krupyanskii, M. G. Mikhailyuk, S. V. Esin, et al., Biophysics 51, 8 (2006).
A. Guinier, X-Ray Diffraction: In Crystals, Imperfect Crystals, and Amorphous Bodies (Dunod, Paris, 1956; Freeman, New York, 1963; Fizmatgiz, Moscow, 1961).
R. W. James, The Optical Principle of the Diffraction of X-Rays (Bell, London, 1950).
A. I. Kitaigorodskii, X-Ray-Structural Analysis of Fine-Crystalline and Amorphous Bodies (Gostekhteoretizdat, Moscow, 1953) [in Russian].
M. Kakudo and N. Kasai, X-Ray Diffraction by Polymers (Elsevier, Amsterdam, London, New York, 1972).
B. E. Warren and N. S. Gingrich, Phys. Rev. 46, 368 (1934).
V. V. Volkov, in Proceedings of the 5th National Conference on Application of X-Ray and Synchrotron Radiation, Neutrons and Electrons for Material Research RSNE-2005 (IK RAN, Moscow, 2005), p. 51.
D. I. Svergun and L. A. Feigin, Small-Angle X-ray and Neutron Scattering (Nauka, Moscow, 1986) [in Russian].
R. L. Messbauer, Khim. Fiz. 1, 1297 (1982).
Yu. F. Krupyanskii, F. Parak, V. I. Goldanskii, et al., Z. Naturforch. 37, 57 (1982).
V. I. Goldanskii and Yu. F. Krupyanskii, Quart. Rev. Biophys. 22, 39 (1989).
Yu. F. Krupyanskii, V. I. Goldanskii, G. U. Nienhaus, and F. Parak, Hyperfine Interact. 53, 59 (1990).
Yu. F. Krupyanskii, K. V. Shaitan, I. V. Kurinov, et al., Biofizika 33, 401 (1988).
Yu. F. Krupyanskii and V. I. Goldanskii, in Proceedings of the International School of Physics “Enrico Fermi” (IOS Press, Amsterdam, 2001), p. 25.
Yu. F. Krupyanskii, P. P. Noks, N. G. Loiko, et al., Biophysics 56, 8 (2011).
J. A. McCammon, Rep. Prog. Phys. 41, 1 (1984).
M. Karplus and G. A. Petsko, Nature 347, 631 (1990).
K. V. Shaitan and K. B. Tereshkina, Molecular Dynamics of Proteins and Peptides (Oikos, Moscow, 2004) [in Russian].
B. Hess, C. Kutzner, D. van der Spoel, et al., J. Chem. Theory Comput. 4, 435 (2008).
A. A. Granovsky, Firefly Vers. 7.1.G. http://classic.chem.msu.su/gran/firefly/index.html
Q. Zou, B. J. Bennion, V. Daggett, and K. P. Murphy, J. Am. Chem. Soc. 124, 1192 (2002).
P. J. Artymiuk, C. C. F. Blake, D. W. Rice, and K. S. Wilson, Acta Crystallogr. 38, 778 (1982).
S. E. Boyce, D. L. Mobley, G. J. Rocklin, et al., J. Mol. Biol. 394, 747 (2009).
A. V. Geliev, Kh. D. Do, B. V. Egorov, et al., Russ. J. Phys. Chem. B 30, 124 (2011).
A. G. Murzin and A. V. Finkelstein, J. Mol. Biol. 204, 749 (1988).
I. G. Plashchina, I. L. Zhuravleva, E. I. Martirosova, et al., Biotechnology, Biodegradation, Water and Foodstuff (Nova Science, New York, 2009), p. 45.
A. Mukherjee, P. Grobelny, T. S. Thakur, and G. R. Desiraju, Cryst. Growth Des. 11, 2637 (2011).
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Original Russian Text © K.B. Tereshkina, A.S. Stepanov, D.O. Sinitsyn, Yu.F. Krupyanskii, 2014, published in Khimicheskaya Fizika, 2014, Vol. 33, No. 7, pp. 64–73.
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Tereshkina, K.B., Stepanov, A.S., Sinitsyn, D.O. et al. Influence of small-molecule ligands and their complexes on lysozyme properties. Russ. J. Phys. Chem. B 8, 534–542 (2014). https://doi.org/10.1134/S1990793114040137
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DOI: https://doi.org/10.1134/S1990793114040137