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Background: Targeting of macromolecules by means of translational diffusion for therapeutic reason is generally of interest. But translational velocity that enables directional delivery of any molecule on target is given less attention.
Objectives: The objectives of this research are to: 1) determine the value of the cohesion factor affecting solutes, 2) determine the translational velocity of porcine pancreatic (PPAA) - and human salivary (HSAA) – alpha amylase and ions, 3) rederive the effective kinetic energy (K.E.) of solutes, 4) determine the thermodynamic parameters for a folded to an unfolded transition and 5) give reasons why the velocity of solution components is generally very important.
Methods: A theoretical research and experimentation using Bernfeld method.
Results and Discussion: The K.E. of solution components as re-derived is « 3kBT / 2 (where kB and T are Boltzmann constant and Kelvin temperature respectively.). The velocities of hydrolysis of the substrate with the sucrose-treated PPAA were generally higher than those of HSAA. The values of conformational entropy change (∆Sconf) for PPAA were generally higher than those of HSAA. Expectedly the values of ∆Sconf were positive.
Conclusion: In conclusion, the square root of the cohesion factor is larger than 22.4 exp (+3) 310.15 K / 273.15 K / 18, accounting for the translational velocity (u) in solution being « gas phase velocity (U). The translational diffusion D and u remain respectively, a function of the hydrodynamic radius of the solutes in particular and the magnitude of D; unfolding of proteins decreases the values of the parameters. Overall, unfolding is entropy driven. Without the mobility of solution components at desired velocity directional delivery of small molecules to site of need such as intrinsically disordered proteins etc may remain impossible.
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