Hot and cold denaturation of proteins: Critical aspects
Niels Bohr Institute and NORDITA, Blegdamsvej 17,
2100 Copenhagen Ø, Denmark
Corresponding author: a Alex.Hansen@phys.ntnu.no
Published online: 15 July 1999
We argue that the first order hot and cold folding transitions of proteins observed at physiological chemical conditions ends in a critical point at a given temperature and chemical potential of the surrounding water. We investigate the properties of this critical point using a single-pathway scenario for the folding process. This pathway assumption determines the form of a Hamiltonian whose critical properties define a new universality class.
PACS: 05.70.Jk – Critical point phenomena / 82.20.Db – Statistical theories (including transition state) / 87.15.By – Structure, bonding, conformation, configuration, and isomerism of biomolecules
© EDP Sciences, Società Italiana di Fisica, Springer-Verlag, 1999