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Like other biomolecules, proteins can also be broken down by high heat alone. At 250 °C, the peptide bond may be easily hydrolyzed, with its half-life dropping to about a minute. [27] [30] Protein may also be broken down without hydrolysis through pyrolysis; small heterocyclic compounds may start to form upon
Whereas the concept of water activity is widely known and utilized in the applied biosciences, its complement—the protein activity which quantitates protein–protein interactions—is much less familiar to bioscientists as it is more difficult to determine in dilute solutions of proteins; protein activity is also much harder to determine for ...
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]
Concentrated nitric acid is added to a protein solution from the side of the test tube to form two layers. A white ring appears between the two layers if the test is positive. [1] Heller's test is commonly used to test for the presence of proteins in urine. [2] This test was discovered by the Austrian Chemist, Johann Florian Heller (1813-1871).
Some MLOs serve their biological role as solid particles (e.g. Balbiani body stabilised by β-sheet structure [23]), but in many cases transformation from liquid to solid results in the formation of pathological aggregates. [24] Examples of both liquid-liquid phase separating and aggregation-prone proteins include FUS, [25] TDP-43 [26] [27] and ...
Crystal structure of β-glucosidase from Thermotoga neapolitana (PDB: 5IDI).Thermostable protein, active at 80°C and with unfolding temperature of 101°C. [1]In materials science and molecular biology, thermostability is the ability of a substance to resist irreversible change in its chemical or physical structure, often by resisting decomposition or polymerization, at a high relative ...
Correct protein folding is integral to proper functionality within biological systems. Hydrophobic collapse is one of the main events necessary for reaching a protein's stable and functional conformation. Proteins perform extremely specific functions which are dependent on their structure. Proteins that do not fold correctly are nonfunctional ...
Coagulation-flocculation process in a water treatment system. In water treatment, coagulation and flocculation involve the addition of compounds that promote the clumping of fine floc into larger floc so that they can be more easily separated from the water. Coagulation is a chemical process that involves neutralization of charge whereas ...