2001 , September, Volume 1, Issue 1, p. 10-11
Ariel Fernández
James Franck Institute & Department of Chemistry, The University
of Chicago, Chicago, Illinois 60637,USA;
Instituto de Matemática,
Universidad Nacional del Sur, Consejo Nacional de Investigaciones Científicas
y Técnicas, Bahía Blanca 8000, Argentina
Protein folding: coming to terms with cooperativity
The standard theoretical approaches to protein folding are inconsistent: the complexity of explicitly treating solvent structure is avoided by treating it implicity using pairwise additive intramolecular potentials, but there are sensitive to the local dielectric strusture created by the protein chain, and hence the intramolecular potential energy must include higher correlations if they are to account for cooperativity. This idea is developed using a simple specific example demonstrating the existence of a "self-kosmotropic" effect in which the chain organizes solvent locally. Which then dramatically affects its own intramolecular interactions.