Hydrophobic charged

The next important phenomena that the result of supramolecular effect are the concentration and proximity effects concerning the components of analytical reaction, even through they are considerably different in hydrophobicity, charge of the species, complexing or collisional type of interaction. The concentration and proximity effects determine the equilibrium of analytical reaction, the efficiencies of intramolecular or intermolecular electronic energy or electron transfer and as a result the sensitivity of analytical reactions. 

Physical-chemical characteristics of prion proteins are evident after assigning different parameters, including hydrophobicity, charge, and molecular weight to the amino acid residues (Inouye and Kirschner, 1991, 1998) (Table II, Fig. 5). The sequences among different animals... 

Egisto B, David J, Warren S, Peter T. Hydrophobic charge induction chromatography, Genet Eng News 2000 20. 

Fig. 2. A schematic view of a protein interacting with a well characterized surface. The protein has a number of surface domains with hydrophobic, charged, and polar character. The solid surface has a similar domain-like...

Klein et al. (1986) reported the compositional or physicochemical properties (attributes) of amino acid sequences in 1603 protein sequences to establish a classification system for 26 protein functions. These results showed that three or four attributes were generally sufficient to distinguish each of the 26 functional categories from the remainder of the database. The attributes used were related to hydrophobicity, charge and its distribution (frequency or... 

Direct attachment of biomolecules to the surface can introduce a steric constraint to reactivity of the molecule which is not encountered when considering molecules free in a solution. This effect can be minimized if, for example, a spacer is introduced between the biomolecule and the linking group. The spacer can be of nearly any desired length and possess a variety of chemical characteristics, that is, it can be rigid or flexible, hydrophilic or hydrophobic, charged or neutral.1,9... 

Complex aminoacid sequences structure Thiophilic like ligands Hydrophobic charge transfer effect... 

Hydrophobic charge induction Mix mode All antibodies Definition of intermediate washings... 

Burton, S. C., and Harding, D. R. (1998). Hydrophobic charge induction chromatography Salt independent protein adsorption and facile elution with aqueous buffers. ]. Chromatogr A 814, 71-81. 

Fig. 13.6. Calculated vs. observed changes in aggregation rates upon mutation. The experimental data relate to mutations of short peptides or natively unfolded proteins including amylin, the A(3-peptide and a-synuclein. The calculated values are determined from an equation involving the changes in just three variables -hydrophobicity, charge and secondary structure propensities - caused by the mutations. The plot shows, for both experimental and calculated data, In (umut/vwt), he., the natural logarithm of the aggregation rate of the mutant umut divided by that of the wild-type molecule vwt. From [36]...

The hydrophobic charge on the interface, which is fundamental for the polymer adsorption, increases with increase in the residual acetate content and the blocky character of acetate groups. This fact is contrary to the aim of wanting large particles because of the simultaneous reduction in interfacial tension [42]. 

Parameters defining the quality of the interface such as enzyme orientation, substrate packing, hydrophobicity, charge density, and film pressure come into consideration [2-4], and terms characterizing enzyme activities such as Vmax and Km have different meanings. 

The behavior of protein molecules at solid surfaces is very complex. The interaction between the surface and the protein is determined both by the nature of the protein, the surface and the medium outside the surface. The situation is further complicated by the fact that exchange reactions between protein molecules of the same or different kinds take place on the surface. Except for these exchange reactions most protein molecules appear to be irreversibly adsorbed. Although the details of the interaction between protein molecules and surfaces are not known it is assumed that general properties of the surface and the protein such as hydrophobicity, charge density, ion binding, hydration etc. are involved. For reviews, see e.g (21.35-37). 

---