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Thermodynamic basis of site‐specific cooperativity
Author(s) -
Cera Enrico Di
Publication year - 1994
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.360340803
Subject(s) - cooperativity , chemistry , allosteric regulation , folding (dsp implementation) , macromolecule , basis (linear algebra) , thermodynamic system , chemical stability , protein folding , thermodynamics , statistical physics , physics , biochemistry , geometry , mathematics , electrical engineering , enzyme , engineering , organic chemistry
Cooperative phenomena in biological macromolecules arise from the interaction of many distinct subsystems, such as structural domains or binding sites. Cooperative properties of the system as a whole, like protein folding or allosteric transitions, are subject to the restrictions imposed by thermodynamic stability. These restrictions, however, do not apply in the case of individual subsystems open to interactions with the rest of the macromolecule. The site‐specific properties of such subsystems can be understood in general thermodynamic terms from those of a multicomponent system under particular conditions. The analogy provides a thermodynamic basis for site‐specific Cooperativity. © 1994 John Wiley & Sons, Inc.