Kinetics and mechanism studies of oxidation of some α-amino acids (Proline, Arginine, Alanine) (AA) by N-Bromosuccinimide (NBS) by using conductivity method was carried out. The kinetic study showed that the reaction was first order with respect to NBS and AA. The effect of addition of HClO 4 to the reaction was negative on the rate of reaction. The reaction was carried outwere calculated. The rate of reaction of AA was as follows: Proline > Arginine > Alanine
The spatial pattern of species is an important feature to understand why these species coexist and remain in position or not, and using the single Ripley function and the L(r) function, we analyzed the spatial pattern of types of broad-leaf tree and tree covers and the needles for mixed brawls in the forests of Mount Gara, using PASSAGE V.2, L(r) analysis of the species under study showed a variation in the pattern distribution of trees and gave the highest percentage of random form distribution pattern with a cluster pattern of 11.25%, Through the ratios and forms of distribution of the L(r) function of the various samples of the study, we find that these stands generally tend to be regular, indicating that these species remain at the end of the life cycle in the structure of a more stable stand.
Cholinesterases are among the most efficient enzymes known. They are divided into two groups: acetylcholinesterase (AChE) involved in the hydrolysis of the neurotransimitter acetylcholine, and butyrylcholinesterase (BChE) of unknown function. Several crystal structures of the former have shown that the active site is located at the bottom of a deep and narrow gorge. Human BChE has attracted attention because it can hydrolyze toxic esters and nerve agents. Here we analyze the complexes of cholinesterase with soman by describing the 3D geometry of the complex, the active site, the changes happened through the inhibition and provide a description for the mechanism of inhibition.
Soman undergoes degradation in the active site of the AChE and BChE. We calculate the energy of the products of the degradation reaction and suggest the reaction path.
The product of the former reaction bind to serine residue in the active site and forming a stable bond and ends the catalytic function of the enzyme.
This study has a useful role in the search of inhibitors to help in the treatment of Alzahimer's disease.
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