Recommanded Product: 20375-65-9, The prevalence of solvent effects in heterogeneous catalysis in condensed media has motivated developing quantitative kinetic and theoretical assessments of solvent structures and their interactions with reaction intermediates and transition states.
Quantitative structure-activity relationships (QSAR) of N-Ac amino acids, N-Ac dipeptides, and N-Ac tripeptides in inhibition of 125I-labeled ristocetin binding to Micrococcus luteus cell wall have been developed to probe the details of the binding between ristocetin and N-acetylated peptides. The correlation equations indicate that (1) the binding is stronger for peptides in which the side chain of the C-terminal amino acid has a large molar refractivity (MR) value, (2) the binding is weaker for peptides with polar than for those with nonpolar C-terminal side chains, (3) the N-terminal amino acid in N-Ac dipeptides contributes 12 times that of the C-terminal amino acid to binding affinity, and (4) the interactions between ristocetin and the N-terminal amino acid of N-acetyl tripeptides appear to be much weaker than those with the first two amino acids.
The potential utility of systematic synthetic strategy will be applicable to efficient generations of chemical libraries of compounds to find ‘hit’ molecules.Read on for other articles about 20375-65-9Recommanded Product: 20375-65-9
Reference：
Pyridazine – Wikipedia,
Pyridazine | C4H4N2673 – PubChem