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The net charge of the protein, determined by the sum charge of its constituents, results in electrophoretic migration in a physiologic electric field. These effects are short-range because of the high di-electric constant of water, however, once the protein is close to a charged surface, electrostatic coupling becomes the dominant force. [8]
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]
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 ...
Protein before and after folding Results of protein folding. Protein folding is the physical process by which a protein, after synthesis by a ribosome as a linear chain of amino acids, changes from an unstable random coil into a more ordered three-dimensional structure. This structure permits the protein to become biologically functional. [1]
The order of the tendency of ions to make or break water structure is the basis of the Hofmeister series. Hofmeister discovered a series of salts that have consistent effects on the solubility of proteins and, as it was discovered later, on the stability of their secondary and tertiary structures.
Thermodynamically the flow of substances from one compartment to another can occur in the direction of a concentration or electrochemical gradient or against it. If the exchange of substances occurs in the direction of the gradient, that is, in the direction of decreasing potential, there is no requirement for an input of energy from outside the system; if, however, the transport is against ...
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 ...
N-terminal acetylation of proteins can affect protein stability, but the results and mechanism were not very clear until now. [23] It was believed that N-terminal acetylation protects proteins from being degraded as Nα-acetylation N-termini were supposed to block N-terminal ubiquitination and subsequent protein degradation. [24]