Charge frequency

Solubility is due to the native structure of proteins. In soluble proteins, hydrophilic parts are located on the outside of the molecule, and the hydrophobic regions are buried. Denaturation induces the insolubility of a protein. According to Bigelow [115], two structural features, hydrophobicity and charge frequency, are the major factors that control the solubility of proteins. 

The protein structure is stabilized by covalent disulphide bonds and a complexity of non-covalent forces, e.g. electrostatic interactions, hydrogen bonds, hydrophobic interactions and van der Waals forces. Both the average hydrophobicity and the charge frequency (parameter of hydrophobicity) are important in determining... 

Here E(t) denotes the applied optical field, and-e andm represent, respectively, the electronic charge and mass. The (angular) frequency oIq defines the resonance of the hamionic component of the response, and y represents a phenomenological damping rate for the oscillator. The nonlinear restoring force has been written in a Taylor expansion the temis + ) correspond to tlie corrections to the hamionic... 

Any charge imbalance in a plasma (i.e. any local deviation from charge neutrality) results in a motion of tire electrons tliat, in turn, leads to oscillations of tire electrons witli tire electron plasma frequency C0p (Langmuir frequency)... 

The Franck-Condon principle reflected in tire connection between optical and tliennal ET also relates to tire participation of high-frequency vibrational degrees of freedom. Charge transfer and resonance Raman intensity bandshape analysis has been used to detennine effective vibrational and solvation parameters [42,43]. 

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