Search results
Results from the WOW.Com Content Network
Substrate dissociation rate contributes to how large or small the enzyme velocity will be. [2] In the Michaelis-Menten model, the enzyme binds to the substrate yielding an enzyme substrate complex, which can either go backwards by dissociating or go forward by forming a product. [2] The dissociation rate constant is defined using K off. [2]
In this table, the more recently published MaxASA values (from Tien et al. 2013 [1]) are systematically larger than the older values (from Miller et al. 1987 [2] or Rose et al. 1985 [3]). This discrepancy can be traced back to the conformation in which the Gly-X-Gly tripeptides are evaluated to calculate MaxASA.
A ligand is "a substance that forms a complex with a biomolecule to serve a biological purpose" (ligand definition), and a macromolecule is a very large molecule, such as a protein, with a complex structure of components (macromolecule definition). Protein-ligand binding typically changes the structure of the target protein, thereby changing ...
The complex is a large integral membrane protein composed of several metal prosthetic sites and 14 [2] protein subunits in mammals. In mammals, eleven subunits are nuclear in origin, and three are synthesized in the mitochondria. The complex contains two hemes, a cytochrome a and cytochrome a 3, and two copper centers, the Cu A and Cu B centers ...
The chelate effect increases as the number of chelate rings increases. For example, the complex [Ni(dien) 2)] 2+ is more stable than the complex [Ni(en) 3)] 2+; both complexes are octahedral with six nitrogen atoms around the nickel ion, but dien (diethylenetriamine, 1,4,7-triazaheptane) is a tridentate ligand and en is bidentate. The number of ...
[2] [3] However, when a medication is administered via routes other than intravenous, its bioavailability is lower due to intestinal epithelium absorption and first-pass metabolism. Thereby, mathematically, bioavailability equals the ratio of comparing the area under the plasma drug concentration curve versus time (AUC) for the extravascular ...
The DSSP algorithm is the standard method for assigning secondary structure to the amino acids of a protein, given the atomic-resolution coordinates of the protein. The abbreviation is only mentioned once in the 1983 paper describing this algorithm, [2] where it is the name of the Pascal program that implements the algorithm Define Secondary Structure of Proteins.
Extreme values of τ 4 and τ 4 ′ denote exactly the same geometries, however τ 4 ′ is always less or equal to τ 4 so the deviation from ideal tetrahedral geometry is more visible. If for tetrahedral complex the value of τ 4 ′ parameter is low, then one should check if there are some additional interactions within coordination sphere.