在水溶液中，是什么决定了配体与蛋白质非共价结合的强度？
What determines the strength of noncovalent association of ligands to proteins in aqueous solution?
作者信息
Miyamoto S, Kollman P A
机构信息
Department of Pharmaceutical Chemistry, University of California, San Francisco 94143.
出版信息
Proc Natl Acad Sci U S A. 1993 Sep 15;90(18):8402-6. doi: 10.1073/pnas.90.18.8402.
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.
使用分子动力学的自由能微扰方法已被用于计算两种配体-蛋白质复合物结合的绝对自由能。与N-L-乙酰色氨酸酰胺/α-胰凝乳蛋白酶相比，这些计算重现了生物素与抗生物素蛋白结合时显著更负的自由能。结合自由能的这种差异是由于抗生物素蛋白呈现给生物素的近乎理想形成的腔中的范德华/色散效应，该腔涉及四个色氨酸残基。
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