Structure proteins factors influencing

The shape of a large protein is influenced by many factors including of course Its primary and secondary structure The disulfide bond shown m Figure 27 18 links Cys 138 of carboxypeptidase A to Cys 161 and contributes to the tertiary structure Car boxypeptidase A contains a Zn " ion which is essential to the catalytic activity of the enzyme and its presence influences the tertiary structure The Zn ion lies near the cen ter of the enzyme where it is coordinated to the imidazole nitrogens of two histidine residues (His 69 His 196) and to the carboxylate side chain of Glu 72... 

Just as the functioning of nucleic acids depends in part on its overall structure, so does the activity of proteins depend on its overall structure. Protein folding is one of the hot areas today in science. To the synthetic polymer chemist, understanding the influences of factors, basic or fundamental, which produce protein chain folding will allow the creation of new synthetic polymers that possess specifically desired properties. For biochemists, understanding these factors allows us to better understand other factors and to combat particular diseases related to chain folding. 

Stability of an enzyme is usually understood to mean temperature stability, although inhibitors, oxygen, an unsuitable pH value, or other factors such as mechanical stress or shear can decisively influence stability (Chapter 17). The thermal stability of a protein, often employed in protein biochemistry, is characterized by the melting temperature Tm, the temperature at which a protein in equilibrium between native (N) and unfolded (U) species, N U, is half unfolded (Chapter 17, Section 17.2). The melting temperature of a protein is influenced on one hand by its amino acid sequence and the number of disulfide bridges and salt pairs, and on the other hand by solvent, added salt type, and added salt concentration. Protein structural stability was found to correlate also with the Hofmeister series (Chapter 3, Section 3.4 Hofmeister, 1888 von Hippel, 1964 Kaushik, 1999) [Eq. (2.18)]. 

Indeed, a direct relationship between the lifetimes of films and foams and the mechanical properties of the adsorption layers has been proven to exist [e.g. 13,39,61-63], A decrease in stability with the increase in surface viscosity and layer strength has been reported in some earlier works. The structural-mechanical factor in the various systems, for instance, in multilayer stratified films, protein systems, liquid crystals, could act in either directions it might stabilise or destabilise them. Hence, quantitative data about the effect of this factor on the kinetics of thinning, ability (or inability) to form equilibrium films, especially black films, response to the external local disturbances, etc. could be derived only when it is considered along with the other stabilising (kinetic and thermodynamic) factors. Similar quantitative relations have not been established yet. Evidence on this influence can be found in [e.g. 2,13,39,44,63-65]. 

The structural differences between the antigen and the host s own version of that protein (self-protein), as well as the host s immunological regulatory mechanisms, are the important factors influencing the outcome of the immune response. 

In many foods, both starch and protein can be encountered so that understanding interactions between them would be useful. The selectivity in interaction between proteins and starches is best seen in results of dynamic rheological studies. The results depend upon the molecular structure of protein, the starch state of the granules and the amylose/amylopectin ratio, the composition of protein and starch, as well as the phase transition temperatures are important factors influencing protein-starch interaction. Because proteins and starches are thermodynamically different polymers, their presence together may lead to phase separation, inversion, or mutual interaction with significant consequences on texture (Morris, 1990). 

The shape of a large protein is influenced by many factors, including, of course, its primary and secondary structure. The disulfide bond shown in Figure 27.18 links Cys-138 of carboxypeptidase A to Cys-161 and contributes to the tertiary structure. Car-... 

Another level of biosynthetic control must derive directly from available genetic information. The genes may exert control in supplying the appropriate information for formation of both structural protein (the proteoglycan protein) and catalytic protein (the specific enzymes responsible for the biosynthetic steps). Tissue culture techniques have also been useful in the examinations of some factors that influence phenotypic characteristics of cells (see S46), and it has been considered (Nl) that proteoglycan and DNA biosynthesis are mutually antagonistic. Such a phenomenon would affect cell differentiation. With the technique of somatic cell hybridization, it has been possible to combine the genomes of two strains of fibroblasts that differ in the rate of production of hyal-... 

In the rat, the observed effects of oral LD50 reflect both the intrinsic toxicity at the ultimate biophase site of action and the factors influencing distribution, membrane transport, protein binding, metabolism and excretion. The manifestation of acute mammalian toxicity is hence a much more complex response than can be described with the use of log alone, although individual processes such as bioavailability and adsorption depend on lipophilic-ity. The fit to a common QSAR model requires that each of these processes has similar structural dependences, qualitatively and quantitatively, within a given class of compounds. If a different process becomes predominant (i.e. rate limiting), the structure-toxicity relationship must alter thus the compound will be an outlier even when the principal mechanism of intrinsic toxicity remains the same. 

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