[Effect of chemical chaperones on properties of lysozyme and the reaction center protein from Rhodobacter sphaeroides].

The influence of three chemical chaperones: glycerol, 4-hexylresorcinol, and 5-methylresorcinol on the structure, equilibrium fluctuations, and the functional activity of the hydrophilic enzyme lysozyme and the transmembrane reaction center (RC) protein from Rb. sphaeroides in a broad range of concentrations has been studied. Selected chemical chaperones are strongly different by the structure and action on hydrophilic and membrane proteins.

[Changes in physicochemical properties of proteins, caused by modification with alkylhydroxybenzenes].

Kinetic characteristics of model enzymes and physicochemical properties of globular proteins modified by chemical analogues of low-molecular-weight microbial autoregulators (alkylhydroxybenzenes, AHBs) have been studied. C7 and C12 AHB homologues were used, differing in the length of the alkyl radical and the capacity for weak physicochemical interactions. Both homologues affected the degree of protein swelling, viscosity, and the degree of hydrophobicity.

[A study of protein structure changes during hydration by means of diffuse X-ray scattering. II. Fourier transform analysis of X-ray scattering data].

Radial distribution functions were deduced by Fourier transform analysis of angular dependences of diffuse x-ray scattering intensities for the following proteins with different hydration degree: water-soluble a-protein myoglobin, water-soluble alpha+beta protein lysozyme, and transmembrane proteins of photosynthetic reaction centers from purple bacteria Rhodobacter sphaeroides and Blastochlorii viridis. The results of Fourier analysis of x-ray scattering intensities give the quantitative characteristics of the mechanisms underlying the influence of water on the formation of biomacromolecules. Water, on the one hand, weakens the intraglobular hydrogen bond net, loosens the protein structure, and increases the internal conformational dynamics.

[A study of protein structure changes during hydration by diffuse X-ray scattering. I. The intensity and the shape of "10-angstrom" maximum].

The angle dependencies of diffuse x-ray scattering intensities were studied in a wide range of angles from 3 to 80 degrees for water-soluble and membrane proteins with a different structural organization: alpha-helical protein myoglobin, alpha-helical protein serum albumen, alpha + beta protein lysozyme, and transmembrane proteins of photosynthetic reaction centers (RC) from purple bacteria Rhodobacter sphaeroides, and Blastochlorii (Rhodopseudomonas) viridis containing cytocrome c, situated out side the membrane, and for H and L+M subunits of membrane protein of reaction center from Rb. sphaeroides for various hydration degrees. The hydration/dehydration process was studied for water-soluble proteins (within hydration range from h = 0.

[Equilibrium fluctuations in myoglobin and lysozyme].

The angular dependencies of inelastic intensities of Rayleigh scattering of Moessbauer radiation were measured for myoglobin and lysozyme (in the hydration range h = 0.05-0.7).

[Comparison of dynamic properties of various globular proteins and polyglutamic acid in alpha-helical and coil states. Rayleigh scattering of Mossbauer radiation data].

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 Rayleigh scattering of Moessbauer radiation technique.

[Study of the dynamics of human serum albumin by coherent Rayleigh dispersion of Mossbauer radiation].

The measurements of angle dependencies of total and elastic Rayleigh scattering of Mossbauer radiation intensities have been performed for human serum albumin (HSA) with hydration degrees h = 0.13 and h = 0.4.

[A study of the effect of solvent composition and viscosity on the molecular dynamics of human serum albumin using Rayleigh scattering of Mössbauer radiation].

By means of RSMR changes of human serum albumen intramolecular mobility by addition of 1.5% and 7.5% of glutar dialdehyde (GD) in concentrated protein solution, heat denaturation of a protein or substitution of water by water-glycerol solvent with amount of water to glycerol: 1 to 2 were studied.

[Evaluation of the contribution of various types of movement of protein globules into effects observed using the Rayleigh scattering of Mössbauer radiation or the Mössbauer absorption spectroscopy].

Conditions (regions of hydration degrees and temperatures) are considered at which effects observed in Rayleigh Scattering of Mössbauer Radiation and Mössbauer Absorption Spectroscopy can be attributed to changes in intramolecular mobility, rather than contribution of different types of motions of macromolecules as a whole.

[Study of protein dynamics using Mössbauer spectroscopy].

Last experimental results of the study of protein dynamics by Mössbauer absorption spectroscopy and Rayleigh scattering of Mössbauer radiation are reviewed. Dynamical properties of proteins following from the theoretical treatment of these data are described.

[Study of the effect of hydration on the dynamics of various globular proteins by Rayleigh scattering of Mössbauer radiation].

Hydration relationships of the elastic scattering fraction of Mössbauer radiation were studied for human serum albumin (HSA), pancreatic trypsin inhibitor and lysozyme within hydration degrees 0 less than or equal to h less than or equal to 0.75 g/g (at T = 295 degrees K) and temperatures 100K less than or equal to T less than or equal to 320 K (for HSA only at h = 0.03; 0.

[Role of conformational sub-states on the reaction capacity of protein molecules].

A review of the recent data on protein dynamics (mainly myoglobin) by X-ray technique, Mössbauer spectroscopy and Rayleigh scattering of Mössbauer radiation is given. The connection between dynamical and functional properties of biological systems are discussed.

[Debye-Waller factor of Rayleigh scattering of Mössbauer radiation at substances with strong conformation motions].

A model was developed to describe conformational motion of macromolecules. A new formula was derived for the Debye-Waller factor in accordance with this model. The model proposes the existence of fluidlike motions of fragments within the volume of some A3.

[Study of chromophore dynamics by means of Rayleigh scattering of Mossbauer radiation].

The temperature dependence of rayleigh scattering of Mössbauer radiation was studied for two samples of the chromatophores with different relative humidity (P/Ps = 0.35 and 0.94).