What determines the strength of noncovalent association of ligands to proteins in aqueous solution?
收藏PubMed Central1993-09-15 更新2026-05-16 收录
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https://pmc.ncbi.nlm.nih.gov/articles/PMC47364/
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资源简介：
Free energy perturbation methods using molecular dynamics have been used to calculate the absolute free energy of association of two ligand-protein complexes. The calculations reproduce the significantly more negative free energy of association of biotin to streptavidin, compared to N-L-acetyltryptophanamide/alpha-chymotrypsin. This difference in free energy of association is due to van der Waals/dispersion effects in the nearly ideally performed cavity that streptavidin presents to biotin, which involves four tryptophan residues. IMAGES:
提供机构：
National Academy of Sciences
创建时间：
1993-09-15
