CONFORMATIONAL ENERGY CALCULATIONS OF ENZYME-SUBSTRATE INTERACTIONS. I. Computation of Preferred Conformations of Some Substrates of α-Chymotrypsin

摘要: Empirical energy calculations are used to determine all low-energy conformations of the isolated α-chymotrypsin substrates N-acetyl-L-phenylalanine amide, N-acetyl-L-tyrosine N-formyl-L-tyrosine and N-acetyl-L-tryptophan amide. The computed in agreement with available experimental data for L-phenylalanyl, L-tyrosyl L-tryptophanyl side chains proteins, NMR X-ray these small peptides. In following papers, certain substrate will be shown bind selectively enzyme chymotrypsin form stable noncovalent enzyme-substrate complexes.