De Bruyne C K, Yde M
Carbohydr Res. 1977 Jun;56(1):153-64. doi: 10.1016/s0008-6215(00)84247-0.
The binding of a series of alkyl 1-thio-beta-D-galactopyranosides to beta-D-galactosidase from E. coli has been investigated. The inhibition constants were compared to the partition coefficients for the transfer of these substrate-analogues from water to 1-octanol. The relationships between the observed binding-constants and the partition coefficients indicate that part of the aglycon group binds to a hydrophobic area that is limited in relation to the length of hydrocarbon chain that can be accomodated. Outside this area, the hydrocarbon chain is only partially desolvated. The main driving-force for binding of the aglycon group is the increase in entropy resulting from the return of water molecules from the more-organized layer around the solute molecule to the bulk-water phase.
对一系列烷基 1-硫代-β-D-吡喃半乳糖苷与大肠杆菌β-D-半乳糖苷酶的结合进行了研究。将抑制常数与这些底物类似物从水转移到 1-辛醇的分配系数进行了比较。观察到的结合常数与分配系数之间的关系表明，部分糖苷配基基团与一个疏水区域结合，该疏水区域相对于可容纳的烃链长度是有限的。在该区域之外，烃链仅部分去溶剂化。糖苷配基基团结合的主要驱动力是由于水分子从溶质分子周围更有序的层返回到本体水相而导致的熵增加。
