Di Cera E
Istituto di Fisica, Universita' Cattolica, Roma, Italy.
J Theor Biol. 1989 Feb 22;136(4):467-74. doi: 10.1016/s0022-5193(89)80158-4.
The principles of linkage thermodynamics are extended to the analysis of individual site binding phenomena in biological macromolecules. A group of thermodynamic potentials is introduced for the description of linkage among the sites. These potentials are isomorphic with Wyman's linkage potentials derived for the description of the mutual interference of different ligands. Thermodynamic stability principles are used to show how they affect individual site binding phenomena and give rise to possible paradoxes.
连锁热力学原理被扩展用于分析生物大分子中单个位点的结合现象。引入了一组热力学势来描述位点之间的连锁。这些势与为描述不同配体的相互干扰而导出的怀曼连锁势同构。利用热力学稳定性原理来展示它们如何影响单个位点的结合现象并引发可能的悖论。