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Mass transfer can take place due to different driving forces. Some of them are: [12] Mass can be transferred by the action of a pressure gradient (pressure diffusion) Forced diffusion occurs because of the action of some external force; Diffusion can be caused by temperature gradients (thermal diffusion)
The folding funnel hypothesis is closely related to the hydrophobic collapse hypothesis, under which the driving force for protein folding is the stabilization associated with the sequestration of hydrophobic amino acid side chains in the interior of the folded protein. This allows the water solvent to maximize its entropy, lowering the total ...
In physical chemistry, the Evans–Polanyi principle (also referred to as the Bell–Evans–Polanyi principle, Brønsted–Evans–Polanyi principle, or Evans–Polanyi–Semenov principle) observes that the difference in activation energy between two reactions of the same family is proportional to the difference of their enthalpy of reaction.
The driving force shown here as ' ' is expressed in units of moles per unit of volume, but in some cases the driving force is represented by other measures of concentration with different units. For example, the driving force may be partial pressures when dealing with mass transfer in a gas phase and thus use units of pressure.
The driving force for mass transfer is usually a difference in chemical potential, when it can be defined, though other thermodynamic gradients may couple to the flow of mass and drive it as well. A chemical species moves from areas of high chemical potential to areas of low chemical potential.
An important concept related to the equilibrium potential is the driving force. Driving force is simply defined as the difference between the actual membrane potential and an ion's equilibrium potential V m − E i {\displaystyle V_{\mathrm {m} }-E_{\mathrm {i} }\ } where E i {\displaystyle E_{\mathrm {i} }\ } refers to the equilibrium ...
The adsorption of larger biomolecules such as proteins is of high physiological relevance, and as such they adsorb with different mechanisms than their molecular or atomic analogs. Some of the major driving forces behind protein adsorption include: surface energy, intermolecular forces, hydrophobicity, and ionic or electrostatic interaction. By ...
The ultimate driving force in self-assembly is energy minimization and the corresponding evolution towards equilibrium, but kinetic effects can also play a very strong role. These kinetic effects, such as trapping in metastable states, slow coarsening kinetics, and pathway-dependent assembly, are often viewed as complications to be overcome in ...