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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]
However among the gene products (gps) necessary for phage assembly, Snustad [34] identified a group of gps that act catalytically rather than being incorporated themselves into the phage structure. These gps were gp26, gp31, gp38, gp51, gp28, and gp4 [gene 4 is synonymous with genes 50 and 65, and thus the gp can be designated gp4(50)(65)].
Although the active site occupies only ~10–20% of the volume of an enzyme, [1]: 19 it is the most important part as it directly catalyzes the chemical reaction. It usually consists of three to four amino acids, while other amino acids within the protein are required to maintain the tertiary structure of the enzymes.
It is important to note that while all non-competitive inhibitors bind the enzyme at allosteric sites (i.e. locations other than its active site)—not all inhibitors that bind at allosteric sites are non-competitive inhibitors. [1] In fact, allosteric inhibitors may act as competitive, non-competitive, or uncompetitive inhibitors. [1]
In chemistry, bifunctionality or difunctionality is the presence of two functional groups in a molecule. A bifunctional species has the properties of each of the two types of functional groups, such as an alcohol (−OH), amide (−CONH 2), aldehyde (−CHO), nitrile (−CN) or carboxylic acid (−COOH). Many bifunctional species are used to ...
Ribonucleotide reductase (RNR), also known as ribonucleoside diphosphate reductase, is an enzyme that catalyzes the formation of deoxyribonucleotides from ribonucleotides. [1] [2] It catalyzes this formation by removing the 2'-hydroxyl group of the ribose ring of nucleoside diphosphates (or triphosphates depending on the class of RNR).
-Enzymes exhibit extreme selectivity towards their substrates. Typically enzymes display three major types of selectivity: Chemoselectivity: Since the purpose of an enzyme is to act on a single type of functional group, other sensitive functionalities, which would normally react to a certain extent under chemical catalysis, survive. As a result ...
These reactions are typically catalysed by enzymes with "histone acetyltransferase" (HAT) or "histone deacetylase" (HDAC) activity. Acetylation is the process where an acetyl functional group is transferred from one molecule (in this case, acetyl coenzyme A) to another. Deacetylation is simply the reverse reaction where an acetyl group is ...