自由能微扰
范德瓦尔斯力
化学
链霉亲和素
生物素
色氨酸
水溶液
糜蛋白酶
分子动力学
生物物理学
计算化学
生物化学
分子
物理化学
氨基酸
酶
生物
有机化学
胰蛋白酶
作者
Shuichi Miyamoto,Peter A. Kollman
标识
DOI:10.1073/pnas.90.18.8402
摘要
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.
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