Molecular interaction, minimal

In order to measure molecular hyperpolarizabilities the now standard D-C induced SHG experiment is used (12). Although it would be more suitable to work in the gas phase to minimize molecular interactions, high molecular weights (low vapour pressure) and chemical decomposition processes make it hardly feasible for the molecules of interest. 

The structure and function of enzymes is determined by both the amino acid sequence and the surrounding solvent. The overall stability of proteins is characterized by a subtle balance of into- and inter-molecular interactions. The basic principle of the structure (and of the stability) of the proteins is related to the nature of its normal enviromnent for (water) soluble globular proteins this is the minimization of the hydrophobic surface area, whereas the contrary is the case for membrane proteins (Jaenicke, 1991). 

Axial perturbation may be taken to indicate the presence of negative charge on the 2-axis, which means that there must be atoms there. From the chemist s point of view it is interesting to know what sort of atoms lie on the axis, and whether they should be regarded as coordinated to the metal or not. Maki (161) proposed that, in solutions of these nickel chelates, all molecules are equally solvated, and that the difference between pyridine and inert solvents is only one of degree. In the melts there must then be some sort of molecular interaction, which does not have more than a minimal effect on the viscosity (222) the melts can be regarded as auto-solutions (221). 

The interaction between components A and B is energetically unfavorable compared to the other two molecular interactions. In this case, the system is immiscible. The phases will separate immediately upon mixing to minimize contact between the two species. 

Del Bene J, Pople JA (1970) Theory of molecular interactions. I. Molecular orbital studies of water polymers using a minimal Slater type basis. J Chem Phys 52 4858-4866... 

How does immobilization stabilize a protein First, it reduces the inter-molecular interaction, thus abolishing aggregation (38). Second, it minimizes the unfolding of the protein molecule by multipoint attachment to the matrix. Thus, the number of attachment bonds between the enzyme and the matrix correlates well with the enhancement in stability achieved as a result of immobilization (39). Mozhaev et al. (39) note that this stabilization cannot be pushed beyond a certain limit because irreversible denaturation is always possible. 

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