Conference publications


XVIII conference

The Influence of Chemical Chaperones on Properties of Lysozyme and Reaction Center Protein from Rb. sphaeroides

Krupyanskii Yu.F., Knox P.P.1, Loiko N.G.2, Abdulnasirov E.G., Stepanov S.A., El'-Registan G.I.2, Rubin A.B.1

Russia, 119997, Moscow, Kosygina,4, ICP RAS

1Russia, 119991, Moscow, Leninskie gory, MSU

2Russia, 119991, Moscow, Av. 60-Years of October 7, b.2, INMI

1 pp. (accepted)

The influence of the following chemical chaperones: glycerol, 4 – hexylresorcinol and 5 – methylresorcinol on the structure, equilibrium fluctuations and functional activity of hydrophilic enzyme lysozyme and transmembrane reaction center (RC) protein from Rb. Sphaeroides was studied in the large variety of their concentrations. Selected chemical chaperones are strongly different by structure and by their action on hydrophilic and membrane proteins. The influence of chemical chaperones (except methylresorcinol) on structure, dynamics and functional properties of lysozyme and RC are well described within the frames of extended models of preferential hydration and preferential interaction of protein with a chemical chaperone. The molecule of hexylresorcinol consists of hydrophobic (alkyl radical) and hydrophilic (aromatic nuclei) parts. This fact provides additional regulation of functional activity of lysozyme and RC by hexylresorcinol. The influence of methylresorcinol on proteins is different from that of glycerol and hexylresocinol. Methylresorcinol interacts with a lysozyme surface directly, not via water hydrogen bonds. This lead to the decrease of denatured temperature Td, to the increase of the amplitude of the equilibrium fluctuation temperature and let him be the powerful activator. Methylresorcinol interacts with membrane protein RC only by means of tightening of hydration water, which is close to be negligible in case of methylresorcinol. Therefore methylresorcinol does not impact functional properties of RC protein. Various chemical chaperones (at the given concentration) and various concentrations of a given chemical chaperone arrange diverse 3D structures of proteins which differ by dynamic and functional characteristics.

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