Protein folding properties, dependence

As is well-known in practice, the protein folding properties and, hence the product quality is dependent on the cultivation conditions of the host organism. Thus, in order to guarantee products within narrow specification limits, the production process must be kept under tight control (4). An essential prerequisite is accurate monitoring of the process state and an optimization of the trajectories of the key process variables. Advanced control strategies require to predict the process behaviour at least over time horizons which are needed to influence the process so that the state variables will not escape from the acceptable intervals. Prediction, however, means that the process has to be modelled. 

The ionic strength dependence of intrinsic viscosity is function of molecular structure and protein folding, ft is well known that the conformational and rheological properties of charged biopolymer solutions are dependent not only upon electrostatic interactions between macromolecules but also upon interactions between biopolymer chains and mobile ions. Due electrostatic interactions the specific viscosity of extremely dilute solutions seems to increase infinitely with decreasing ionic concentration. Variations of the intrinsic viscosity of a charged polyampholite with ionic strength have problems of characterization. 

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. 

Once it has started folding, the protein eventually tightens into a specific three-dimensional shape, called its tertiary structure. Just like humans have unique sets of fingerprints, every protein has a unique tertiary structure, which is responsible for its properties and function. The tertiary structure is held together by bonds between the R groups of the amino acids in the protein, and so depends on the amino acid sequence. There are three kinds of bonds involved in tertiary protein structure ... 

The distribution properties shown in Fig. 6 strongly depend on protein folding (dependence of hit rates). In practice, a-helix-rich protein has a smoother distribution. This is because of the smaller potential energy barrier of steric repulsion, which results in faster conformational space search (Fig. 5B). The procedure of Fig. 4 can be applied to the proteins with relatively few iterations and short calculation time.66,67... 

The efficiency of protein/chromophore maturation is an intrinsic property of each fluorescent protein or mutant thereof. With respect to this, time, temperature, oxygen-availability and the intrinsic rates of cyclization/oxidation during chromophore formation play important roles [51]. As outlined in this review the latter is strictly dependent on the specific interaction between the chromophore residues and the environmental amino-acid side-chains provided by the 6-can protein backbone. Availability of chaperonins can be helpful [105] but is not required. In case of fusions between host proteins and a fluorescent protein hindrance of the protein folding thus preventing proper maturation can not be excluded. This can only by tested empirically. 

Force fields must be relatively simple and computationally efficient for studying complex macromolecules such as proteins and DNAs. The force fields usually describe properties of certain types better than others, depending on how the force fields were developed. We have already learned from the sensitivity analysis studies of liquid water and a two-dimensional square lattice model of protein folding that different system properties can be determined by different features of a potential model. 

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