https://doi.org/10.1007/s100510050537
Statistical mechanics of warm and cold unfolding in proteins
Niels Bohr Institute and NORDITA, Blegdamsvej 17, 2100,
Denmark
Corresponding author: a mhjensen@nbi.dk
Received:
19
March
1998
Accepted:
25
May
1998
Published online: 15 November 1998
We present a statistical mechanics treatment of the stability of globular proteins which takes explicitly into account the coupling between the protein and water degrees of freedom. This allows us to describe both the cold and the warm unfolding, thus qualitatively reproducing the known thermodynamics of proteins.
PACS: 87.10.+e – General, theoretical, and mathematical biophysics (including logic of biosystems, quantum biology, and relevant aspects of thermodynamics, information theory, cybernetics, and bionics) / 05.70.Jk – Critical point phenomena / 82.20.Db – Statistical theories (including transition state)
© EDP Sciences, Società Italiana di Fisica, Springer-Verlag, 1998
