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where is the stability of the protein in water and [D] is the denaturant concentration. Thus the analysis of denaturation data with this model requires 7 parameters: Δ G w {\displaystyle \Delta G_{w}} , Δ n {\displaystyle \Delta n} , k , and the slopes and intercepts of the folded and unfolded state baselines.
Protein precipitation is widely used in downstream processing of biological products in order to concentrate proteins and purify them from various contaminants. For example, in the biotechnology industry protein precipitation is used to eliminate contaminants commonly contained in blood. [1]
Many medical devices and products come into contact with the internal surfaces of the body, such as surgical tools and implants. When a non-native material enters the body, the first step of the immune response takes place and host extracellular matrix and plasma proteins aggregate to the material in attempts to contain, neutralize, or wall-off the injurious agent. [1]
Ions that have a strong "salting in" effect such as I − and SCN − are strong denaturants, because they salt in the peptide group, and thus interact much more strongly with the unfolded form of a protein than with its native form. Consequently, they shift the chemical equilibrium of the unfolding reaction towards unfolded protein. [17]
When a protein folds, the titratable amino acids in the protein are transferred from a solution-like environment to an environment determined by the 3-dimensional structure of the protein. For example, in an unfolded protein, an aspartic acid typically is in an environment which exposes the titratable side chain to water.
Mass transfer is the net movement of mass from one location (usually meaning stream, phase, fraction, or component) to another.Mass transfer occurs in many processes, such as absorption, evaporation, drying, precipitation, membrane filtration, and distillation.
The presence of multiple domains in proteins gives rise to a great deal of flexibility and mobility, leading to protein domain dynamics. [1] Domain motions can be inferred by comparing different structures of a protein (as in Database of Molecular Motions ), or they can be directly observed using spectra [ 12 ] [ 13 ] measured by neutron spin ...
Stability of beta barrel (β-barrel) transmembrane proteins is similar to stability of water-soluble proteins, based on chemical denaturation studies. Some of them are very stable even in chaotropic agents and high temperature. Their folding in vivo is facilitated by water-soluble chaperones, such as protein Skp. It is thought that β-barrel ...