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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]
Enzymes (/ ˈ ɛ n z aɪ m z /) are proteins that act as biological catalysts by accelerating chemical reactions.The molecules upon which enzymes may act are called substrates, and the enzyme converts the substrates into different molecules known as products.
Cyanobacteria such as these carry out photosynthesis.Their emergence foreshadowed the evolution of many photosynthetic plants and oxygenated Earth's atmosphere.. Biological carbon fixation, or сarbon assimilation, is the process by which living organisms convert inorganic carbon (particularly carbon dioxide, CO 2) to organic compounds.
Ribbon diagram of a protease (TEV protease) complexed with its peptide substrate in black with catalytic residues in red.(. A protease (also called a peptidase, proteinase, or proteolytic enzyme) [1] is an enzyme that catalyzes proteolysis, breaking down proteins into smaller polypeptides or single amino acids, and spurring the formation of new protein products. [2]
At high temperatures, these interactions cannot form, and a functional protein is denatured. [25] However, it relies on two factors; the type of protein used and the amount of heat applied. The amount of heat applied determines whether this change in protein is permanent or if it can be transformed back to its original form. [26]
Nitrogenase is an enzyme responsible for catalyzing nitrogen fixation, which is the reduction of nitrogen (N 2) to ammonia (NH 3) and a process vital to sustaining life on Earth. [9] There are three types of nitrogenase found in various nitrogen-fixing bacteria: molybdenum (Mo) nitrogenase, vanadium (V) nitrogenase , and iron-only (Fe ...
There is a strong plausibility of the development of antibiotics that would attack the glyoxylate cycle, which would kill the disease-causing microorganisms that depend on the cycle for their survival, yet would not harm humans where the cycle, and thus the enzymes that the antibiotic would target, are absent. [2]
Different proteins are degraded at different rates. Abnormal proteins are quickly degraded, whereas the rate of degradation of normal proteins may vary widely depending on their functions. Enzymes at important metabolic control points may be degraded much faster than those enzymes whose activity is largely constant under all physiological ...