Protein compressibility, dynamics, and pressure.
The relationship between the elastic and dynamic properties of native globular proteins is considered on the basis of a wide set of reported experimental data. The formation of a small cavity, capable of accommodating water, in the protein interior is associated with the elastic deformation, whose contribution to the free energy considerably exceeds the heat motion energy. Mechanically, the protein molecule is a highly nonlinear system. This means that its compressibility sharply decreases upon compression. The mechanical nonlinearity results in the following consequences related to the intramolecular dynamics of proteins: 1) The sign of the electrostriction effect in the protein matrix is opposite that observed in liquids-this is an additional indication that protein behaves like a solid particle. 2) The diffusion of an ion from the solvent to the interior of a protein should depend on pressure nonmonotonically: at low pressure diffusion is suppressed, while at high pressure it is enhanced. Such behavior is expected to display itself in any dynamic process depending on ion diffusion. Qualitative and quantitative expectations ensuing from the mechanical properties are concordant with the available experimental data on hydrogen exchange in native proteins at ambient and high pressure.
Kharakoz
D P
DP
Institute of Theoretical and Experimental Biophysics, Russian Academy of Science, 142290 Pushchino, Moscow, Russia. kharakoz@pbc.iteb.serpukhov.su
D019245:Compressive Strength / Q000502:physiology; D004548:Elasticity; D004735:Energy Transfer / Q000502:physiology; D006859:Hydrogen / Q000737:chemistry; D007477:Ions; D009682:Magnetic Resonance Spectroscopy; D008956:Models, Chemical; D017711:Nonlinear Dynamics; D011312:Pressure; D011506:Proteins / Q000737:chemistry* / Q000502:physiology; D015204:Spectroscopy, Mossbauer; D055672:Static Electricity
D007477:Ions; D011506:Proteins; D006859:Hydrogen