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In biochemistry, denaturation is a process in which proteins or nucleic acids lose folded structure present in their native state due to various factors, including application of some external stress or compound, such as a strong acid or base, a concentrated inorganic salt, an organic solvent (e.g., alcohol or chloroform), agitation and radiation, or heat. [3]
Homeostatic control can change the P CO 2 and hence the pH of the arterial plasma within a few seconds. [5] The partial pressure of carbon dioxide in the arterial blood is monitored by the central chemoreceptors of the medulla oblongata. [5] [20] These chemoreceptors are sensitive to the levels of carbon dioxide and pH in the cerebrospinal ...
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 lack of oxygen (hypoxia) causes cell death in a localized area which is perfused by blood vessels failing to deliver primarily oxygen, but also other important nutrients. While ischemia in most tissues of the body will cause coagulative necrosis, in the central nervous system ischemia causes liquefactive necrosis , as there is very little ...
The condition is believed to be caused by abnormal muscle metabolism following slaughter, due to an altered rate of glycolysis and a low pH within the muscle fibers. A mutation point in the ryanodine receptor gene (RYR1) in pork, [1] associated to stress levels prior to slaughter are known to increase the incidence of PSE meat. Although the ...
A thermal shift assay (TSA) measures changes in the thermal denaturation temperature and hence stability of a protein under varying conditions such as variations in drug concentration, buffer formulation (pH or ionic strength), redox potential, or sequence mutation. The most common method for measuring protein thermal shifts is differential ...
Albumin is commonly used to replenish and maintain blood volume after traumatic injury, during surgery, and during plasma exchange. [3] Since albumin is the most abundant protein in the plasma its use may be the most well known, but many other proteins, although present in low concentrations, can have important clinical uses. [1] See table ...
Extreme temperatures can weaken and destabilize the non-covalent interactions between the amino acid residues. pHs outside of the protein's pH range can change the protonation state of the amino acids, which can increase or decrease the non-covalent interactions. This can also lead to less stable interactions and result in protein unfolding.