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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]
Protein adsorption and protein fouling can cause major problems in the food industry (particularly the dairy industry) when proteins from food adsorb to processing surfaces, such as stainless steel or plastic (e.g. polypropylene). Protein fouling is the gathering of protein aggregates on a surface.
At high concentrations, sorbitan monooleate can increase the viscosity of the emulsion, which can further enhance stability by reducing the movement of dispersed droplets. [ 5 ] When combined with other surfactants, especially those with higher HLB values like Tween 80, sorbitan monooleate can contribute to the overall stability of oil-in-water ...
Other factors suspected to affect degradation rate include the rate deamination of glutamine and asparagine and oxidation of cystein, histidine, and methionine, the absence of stabilizing ligands, the presence of attached carbohydrate or phosphate groups, the presence of free α-amino group, the negative charge of protein, and the flexibility ...
Protein quality is the digestibility and quantity of essential amino acids for providing the proteins in correct ratios for human consumption. There are various methods that rank the quality of different types of protein , some of which are outdated and no longer in use, or not considered as useful as they once were thought to be.
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. Anions appear to have a larger effect than cations , [ 6 ] and are usually ordered as follows: [ 5 ] [ 7 ] [ 8 ]
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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]