Yu. F. Krupyanskii

Russian Academy of Sciences, Moskva, Moscow, Russia

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Publications (26)15.59 Total impact

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    Yu. I. Petrov, EA Shafranovskii, Yu. F. Krupyanskii, S. V. Esin
    Doklady Physical Chemistry 10/2004; 399(1):269-274. DOI:10.1023/B:DOPC.0000048072.90537.79 · 0.48 Impact Factor
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    Yu F Krupyanskii, S V Esin, G V Eshenko, M G Mikhailyuk
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    ABSTRACT: The angular dependencies of inelastic intensities of Rayleigh scatteringof Moessbauer radiation were measured for lysozyme and myoglobin (fordifferent degrees of hydration: from h = 0.05 till h = 0.7). The treating ofthe data at h > 0.05 approves the existence of segmental motions(α-helices for myoglobin, α-helices and β-sheets forlysozyme) as well as of individual motions. Further hydration increase themean-square displacements for both types of intraglobular motions for theseproteins, while the motions of the globule as a whole remain nearlythe same as for h = 0.05. Results of the study of the radial distributionfunction deduced by Fourier - transform from the diffuse x-raymeasurements together with RSMR data allow to conclude that the waterduring hydration of proteins competes with the intramolecular hydrogenbonds, loosens the protein and increases the internal dynamics. At the sametime water arranges the ordering of macromolecule from `glassy' state ath ≈ 0.02 to the native state at h = 0.4-0.7. Differentarchitecture of proteins leads to the different structural dynamics as in thecase of lysozyme and myoglobin.
    Journal of Biological Physics 06/2002; 28(2):139-45. DOI:10.1023/A:1019934304686 · 1.15 Impact Factor
  • Y.F. Krupyanskii, S.V. Esin, G.V. Eshenko, M.G. Mikhailyuk
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    ABSTRACT: The angular dependencies of inelastic intensities of Rayleigh scattering of Mössbauer radiation were measured for lysozyme and myoglobin (for different degrees of hydration: from h=0.05 till h=0.7). The treating of the data at h>0.05 approves the existence of segmental motions (α-helices for myoglobin, α-helices and -sheets for lysozyme) as well as of individual motions. Further hydration increases the mean-square displacements for both types of intraglobular motions for these proteins, while the motions of the globule as a whole remain nearly the same as for h=0.05. Results of the study of the radial distribution function deduced by Fourier-transform from the diffuse X-ray measurements together with RSMR data allow to conclude that the water during hydration of proteins competes with the intramolecular hydrogen bonds, loosens the protein and increases the internal dynamics. At the same time water arranges the ordering of macromolecule from “glassy” state at h≈0.02 to the native state at h=0.4–0.7. Different architecture of proteins leads to the different structural dynamics as in the case of lysozyme and myoglobin.
    Hyperfine Interactions 01/2002; 141. · 0.21 Impact Factor
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    ABSTRACT: The structure and hyperfine fields of Fe1−xCrx (x=0.0236–0.803) nanoparticles (average size of 27±2 nm) are studied at room temperature by combined x-ray diffraction and Mössbauer spectroscopy techniques. They are produced by fast evaporation of bulk alloys at 3 Torr Ar pressure. The bulk alloys of any composition are shown to exhibit a bcc structure, whereas the nanoparticles demonstrate a mixture of bcc and tetragonal σ phases in the Cr range from 24.4 to 83.03 at. %. At the Cr content of 2.36 at. % the lattice constant for nanoparticles is larger than that of the bulk alloy, though the values of hyperfine fields on Fe nuclei do not differ. The Mössbauer spectrum of nanoparticles contains an oxide doublet in addition to the sextet specific to that of the bulk alloy. In both cases the width of the sextet lines is rather narrow. However, even at ∼8 at. % Cr the lines of the sextet are broadened so much that it can be decomposed by two-three components. This is explained by freezing the high-temperature ferromagnetic fcc phase regions in the bcc lattice. As the Cr content increases, the Mössbauer spectra become more complex, transforming finally into a paramagnetic singlet. A complete ferromagnetic→paramagnetic transition is observed for the bulk alloy at 68 at. % Cr and for nanoparticles at 35 at. % Cr. The results are discussed under the assumption that at high temperatures the alloys are not homogeneous and exhibit fluctuations of the composition. With decrease of temperature these fluctuations result in decomposition of the alloy into two phases for nanoparticles whereas they are frozen at the cluster level in the bulk alloys holding a macroscopic homogeneity. © 2002 American Institute of Physics.
    Journal of Applied Physics 12/2001; 91(1):352-361. DOI:10.1063/1.1415367 · 2.21 Impact Factor
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    Doklady Physical Chemistry 06/2001; 379(1):194-198. DOI:10.1023/A:1019242231460 · 0.48 Impact Factor
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    ABSTRACT: Protein specific modes of motions are found in myoglobin crystals above 180 K. In this contribution we show that this type of motions can be analyzed by a Davidson-Cole, a Cole-Cole or a Havriliak-Negami distribution in analogy to dielectric relaxation. However, the temperature dependence of the obtained parameters is quite unusual indicating a broadening of the distributions with temperature instead of motional narrowing. This can be understood from the picture of conformational substates if one assumes that more and more substates become accessible with increasing temperature. The result shows that the analogy between glass forming organic liquids and proteins should not be exaggerated.
    Chemical Physics 11/1996; 212(1):221-229. DOI:10.1016/S0301-0104(96)00182-6 · 2.03 Impact Factor
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    ABSTRACT: Summary The classical model system poly-L-glutamic acid (poly-Glu), was investigated in a disordered coil state (at pH=7.0) and in helix state (at pH=2.0) by the RSMR technique. By considering that the coil state of poly-Glu models unfolded (random coil) state and α-helix state models the fluctuating secondary structure (during consequent folding of protein), a comparative analysis of the dynamical properties of poly-Glu in different states with the dynamical properties of different proteins in the native state (α-helical myoglobin and HSA, partially β-sheet lysozyme) and in intermediate (molten globule) state (α-lactalbumin) was performed. This comparison brings some unpredicted results: native α-helical proteins behave close to random coil, native partially β-sheet proteins behave close to fluctuating secondary structure (α-helix) and the dynamic behaviour of molten-globule state (partially β-sheet α-lactalbumin) is not different from the behaviour of lysozyme and much more rigid than that of native α-helical proteins.
    Il Nuovo Cimento D 02/1996; 18(2):365-369. DOI:10.1007/BF02458919
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    ABSTRACT: The method of differential diathermic calorimetry was used to obtain the curves of release and absorption of heat in water—protein systems. The influences of the rates of cooling and heating and the influence of annealing on the state of a water—lysozyme system at different hydration degrees h = 0.1−0.7 g/g were studied. Experiments have demonstrated that at considerably large rates of cooling there are observed the effects of vitrification of water—protein systems, i.e. the stabilization of a metastable, nonequilibrium structure of system. Decrease of the cooling rate or annealing transforms more of the system into an equilibrium state, increasing the degree of globular crystallinity to more than 70%. Therefore low-temperature experiments with water—protein systems aimed at obtaining functionally important information (i.e. important also at room temperatures) should be performed with slowly cooled or with annealed systems.
    Chemical Physics Letters 06/1993; 208:1-4. DOI:10.1016/0009-2614(93)80066-X · 1.99 Impact Factor
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    ABSTRACT: A comparative study of a native and molten globule state of α-lactalbumin and polyglutamic acid in helical and coiled states were performed by RSMR. Molten globule state possesses the same dynamical features registrated by RSMR as the native one. Large-scale low-frequency motions were registrated in the coiled molecule without any elements of secondary structure.
    Hyperfine Interactions 11/1991; 67(1):597-601. DOI:10.1007/BF02398206 · 0.21 Impact Factor
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    ABSTRACT: In this survey, the scales and correlation times of the motion of iron atoms in the active site of myoglobin and hemoglobin, in the iron containing core, in iron storage proteins, and model polymer systems, and the average fragmental motion of protein globules of myoglobin and human serum albumin are considered. Models of intramolecular protein mobility are presented.
    Hyperfine Interactions 11/1991; 66(1):177-189. DOI:10.1007/BF02395866 · 0.21 Impact Factor
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    ABSTRACT: In the survey, the scales and correlation times of motion on different levels are considered: iron atoms in active centre of myoglobin and hemoglobin, iron containing core in iron storage proteins and model polymer systems, and the average fragmental motion of a protein globule of myoglobin and human serum albumin. The models of intramolecular protein mobility have been drawn.
    Applied Magnetic Resonance 12/1990; 1(3):463-481. DOI:10.1007/BF03166027 · 1.15 Impact Factor
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    ABSTRACT: Recent experimental results on the study of intramolecular mobility of hydrated DNA by RSMR are presented. Hydrated DNA possesses a well-developed mobility: X 2> reaches 1.2 2 at high hydration degree. RSMR spectra were measured for hydrated DNA within a temperature range of 90 K-300 K. A quasielastic “wide” component was observed atT>260 K. Three different types of intramolecular mobility were introduced for description of experimental data.
    Hyperfine Interactions 07/1990; 58(1):2355-2357. DOI:10.1007/BF02398343 · 0.21 Impact Factor
  • Yu. F. Krupyanskii, V. I. Goldanskii, G. U. Nienhaus, F. Parak
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    ABSTRACT: A critical review of recent studies of protein dynamics by the RSMR technique is given. The main approximations in quantitative analyses of RSMR data are discussed and conclusions about dynamical properties of protein and interprotein water, deduced from experiments, are described.
    Hyperfine Interactions 01/1990; 53(1):59-73. DOI:10.1007/BF02101039 · 0.21 Impact Factor
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    ABSTRACT: A method of Mössbauer Fourier spectroscopy is developed to determine the correlation function of coordinates of a macromolecular system. The method does not require the use of an a priori dynamic model. The application of the method to the analysis of RSMR data for human serum albumin has demonstrated considerable changes in the dynamic behavior of the protein globule when the temperature is changed from 270 to 310 K. The main conclusions of the present work is the simultaneous observation of low-frequency (τ≥10−9 sec) and high-frequency (τ≪10−9 sec) large-scaled motions, that is the two-humped distribution of correlation times of protein motions.
    Hyperfine Interactions 11/1988; 39(4):369-378. DOI:10.1007/BF02397646 · 0.21 Impact Factor
  • I.P. Suzdalev, Yu.F. Krupyanskii, V.I. Goldanskii
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    ABSTRACT: Data on the electronic state of iron in active centres of heme proteins and on the dynamics of these proteins have been obtained by means of Mössbauer spectroscopy and Rayleigh scattering of Mössbauer radiation. The influence of conformational rearrangements of the protein globule on the electronic state of the iron atom is considered. Mean square displacements of the iron atom and average mean square displacements of the myoglobin globule are compared.
    Journal of Molecular Catalysis 09/1988; 47(2-3):179-186. DOI:10.1016/0304-5102(88)85041-7
  • V. I. Goldanskii, Yu. F. Krupyanskii
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    ABSTRACT: A review of recent experimental results on the study of protein dynamics by the Rayleigh scattering of Mössbauer radiation (RSMR) method is given. Dynamical properties of protein and protein-bound water, deduced from a quantitative analysis of RSMR data, are described.
    Hyperfine Interactions 01/1988; 39(4):341-358. DOI:10.1007/BF02397644 · 0.21 Impact Factor
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    ABSTRACT: The dependence of the Mössbauer elastic scattering fraction on the hydration degree (h) has been studied for hydrated samples of human albumen (HSA), lysozyme and trypsin pancreatic inhibitor, within the range ofh between 0–0.75 g H2O/g protein at 295 K, and for HSA with different hydration degrees (0.03, 0.25, 0.41, 0.65) in the temperature range between 100–320 K. An increase of the hydration degree forh>0.1 atT>200 K has been shown to result in the release of intramolecular mobility in proteins.
    Hyperfine Interactions 02/1987; 33(1):223-232. DOI:10.1007/BF02394110 · 0.21 Impact Factor
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    V I Gol'danskii, Yu F Krupyanskii, V N Fleurov
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    ABSTRACT: Specific features of the Rayleigh Scattering of Mössbauer Radiation (RSMR) technique in the study of biological systems are described. Experimental data show that the temperature and hydration degree are the principal parameters which influence intramolecular mobility in biopolymers. Data on temperature dependencies of elastic fraction, f, and spectrum line-shape do not fit neither Debye or Einstein models of solids nor the free diffusion in liquids and demand for their explanation a multimode approximation (i.e. a wide spectrum of correlation times, at T = 293 K from 10-6 s to 10-12-10-13 s). On the basis of RSMR, low temperature specific heat and X-ray dynamic analysis data and from the general conditions that information macromolecule must be in a non-equilibrium state (an independent confirmation of this fact comes from the kinetic model of protein folding) a glass-like dynamical model of biopolymers is formulated. A possible interpretation of RSMR data shows that fluctuatively prepared tunneling between quasiequilibrium positions (QEP) can prevail activated transitions up to a room temperature.
    Physica Scripta 06/1986; 33:527. DOI:10.1088/0031-8949/33/6/008 · 1.03 Impact Factor
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    ABSTRACT: Chromatophores from Ectothiorhodospira Shaposhnikovii in solvents of different viscosity were investigated by RSMR experiments in the temperature range between 112 K and room temperature. Additional RSMR-experiments were done on solvents only. The mobility of the molecules and within the molecules is the given by the Debye-Waller factor which yields the meansquare displacement, [`( x2 )]\overline {\left\langle {x^2 } \right\rangle } , averaged over the atoms in the system. The mobility of the atoms of the chromatophores roughly follows the mobility of the atoms of the solvents. At low temperatures the mobility of the chromatophores remains slightly larger than the mobility of the frozen solvent. At room temperature, however, [`( x2 )]\overline {\left\langle {x^2 } \right\rangle } of the chromatophores remains significantly smaller.Chromatophores in a glycerol-water mixture (0.001 M Tris-HCl buffer) and in water (0.05 M Tris-HCl buffer) show a different dynamic behaviour. A region with enhanced mobility near T=180 K was indicated for the chromatophores in the glycerolwater mixture.A correlation has been suggested between the rate of electron transfer from the primary to the secondary quinone and the increase of the conformational mobility of the chromatophores in glycerol-water mixture.
    European Biophysics Journal 05/1985; 12(2):107-114. DOI:10.1007/BF00260433 · 2.47 Impact Factor
  • Le Journal de Physique Colloques 01/1980; DOI:10.1051/jphyscol:19801193

Publication Stats

131 Citations
15.59 Total Impact Points

Institutions

  • 1985–2004
    • Russian Academy of Sciences
      • • N. N. Semenov Institute of Chemical Physics
      • • Institute of Chemistry
      Moskva, Moscow, Russia
  • 2002
    • Semenov Institute of Chemical Physics
      Moskva, Moscow, Russia
  • 1990
    • Moscow Institute of Physics and Technology
      Moskva, Moscow, Russia