A quantitative measure of electrostatic host-guest complementarity, as defined by Umeyama and co-workers and slightly modified by us, is used to characterise the packing of sulphur-containing macrocycles in a crystalline environment. Molecular graphics studies and a semi-quantitative analysis indicate that, at least partly, electrostatic stabilisation emerging from complementarity accounts for the formation of relatively energy rich structures in the crystal. The better is the complementarity with the crystalline environment the higher is the energy of a ring in the solid state as compared to the absolute minimum in the gas phase. A further interesting case of complementarity is the electrostatic fit between enzyme active sites and their protein environment. The (-+ -) charge pattern, characterising the active sites of a number of hydrolytic enzymes, is stabilised by the electrostatic pattern provided by the surrounding protein. It was found that the measure of the electrostatic complementarity between the active site and the environment correlates well with the experimentally determined activities. On this basis we propose to use this measure for the characterisation of enzyme catalytic power.
|Number of pages||8|
|Publication status||Published - Dec 1 2001|
ASJC Scopus subject areas
- Computer Science Applications
- Computational Theory and Mathematics
- Applied Mathematics