Evgenii Permiakov

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Unlike wild type recoverin with only two (the second and the third) functioning Ca(2+)-binding sites out of four potential ones, the +EF4 mutant contains a third active Ca(2+)-binding site. This site was reconstructed from the fourth potential Ca(2+)-binding domain by the introduction of several amino acid substitutions in it by site-directed mutagenesis.(More)
Dissociation kinetics of parvalbumin complexes with calcium and magnesium ions were studied by means of stopped-flow method employing intrinsic protein fluorescence registration. In the temperature range from 10 to 30 degrees C the kinetic curves of Ca2+ and Mg2+ dissociation are best fitted with a sum of two exponential terms, each term is ascribed to a(More)
Physico-chemical properties of troponin I and troponin T subunits from cardiac and skeletal muscles were studied, using intrinsic protein fluorescence and differential scanning microcalorimetry. The effects of temperature, pH, urea and ionic strength were analyzed. Similar skeletal and cardiac components were shown to possess similar properties. Alkali(More)
Electron-vibrational spectra of phosphorescence and fluorescence of tryptophan residues in proteins at 77 K are best approximated by theoretical curves computed according to a model which suggests the existence of two independent series of Gaussian vibrational components. Each series contains one type of vibrations. Phosphorescence and fluorescence spectra(More)
Interactions of the calcium binding proteins, parvalbumin from cod muscles, alpha-lactalbumin from cow milk and calmodulin from bovine brain, with Cu2+ and Zn2+ ions have been studied by intrinsic fluorescence and microcalorimetry methods. It was revealed that parvalbumin binds one Cu2+ ion per molecule with association constant from 10(5) to 10(6) M-1.(More)
Using differential scanning microcalorimetry and measurements of protein fluorescence, the thermal denaturation of lactate dehydrogenase (LDH) from porcine muscle (in the apo-form as well as in the form of the enzyme-pyruvate, enzyme-NAD+ and enzyme-NAD-pyruvate-adduct complexes) was studied. Pyruvate binding did not affect the thermal stability of LDH.(More)
Binding of Ca2+ ion to bovine alpha-lactalbumin molecule causes a conformational change reflected in an almost two-fold decrease of the fluorescence quantum yield and a rather pronounced spectral shift towards shorter wavelengths (by ca. 20 nm). The changes could be interpreted as a result of a transfer of highly exposed tryptophan residue(s) into a rigid(More)
It was found that pike parvalbumins pI 4.2 and 5.0 bind amphiphilic peptide melittin extracted from bee venom in an extraordinary Ca-dependent manner: in apo-state the protein forms a tight equimolar complex with melittin (Ka = 10(6) M-1 at 18 degrees C); in Ca- (and Mg-) loaded state it does not take place. Heating of the protein up to temperatures above(More)
Highly reactive hydrophilic (i.e., water-soluble) p-sulfotetrafluorophenyl esters (Tfs esters) are proposed for peptide synthesis in aqueous and aqueous-organic media, as well as for protein and peptide partial synthesis in an aqueous medium. These esters can serve as a basis for creating a series of protein modifying reagents. As they are analogs of the(More)