TEMPERATURE-INDUCED COMPLEMENTARITY AS A MECHANISM FOR BIOMOLECULAR ASSEMBLY

Recent advances in the measurement and theory of ''hydration'' interac tions between biomolecules provide a basis on which to formulate mecha nisms of biomolecular recognition. In this paper we have developed a m athematical formalism for analyzing specificity encoded in dynamic dis tributions of surface polar groups, a formalism that incorporates newl y recognized properties of directly measured ''hydration'' forces. As expected, attraction between surfaces requires complementary patterns of surface polar groups. In contrast to usual expectations, thermal mo tion can create these complementary surface configurations. We have de monstrated that assembly can occur with an increase in conformational entropy of polar residues. Elevated temperature then facilitates recog nition rather than hinders it. This mechanism might underlie some temp erature-favored assembly reactions common in biological systems that a re usually associated with the ''hydrophobic effect'' only. (C) 1994 W iley-Liss, Inc.