Protein phase diagrams: the physics behind their elliptic shape.
We relate the condition for the elliptic shape of the phase diagram of proteins to the degree of correlation in the fluctuations of the changes of enthalpy and volume at the denaturing-refolding transition. Since this degree cannot be larger than 1, hyperbolically shaped diagrams are not likely to exist. Experiments show that the correlation factor is actually quite low for proteins implying that one-order parameter is not enough to describe the folding-denaturing transition. These findings seem to be the thermodynamic manifestation of the glasslike properties of proteins despite the fact that the transition itself is of first order.
Lesch
Harald
H
Physik Department E14, Lehrstuhl für Physik Weihenstephan, Technische Universität München, An der Saatzucht 5, D-85350 Freising, Germany.
Hecht
Christoph
C
Friedrich
Josef
J
D002626:Chemistry, Pharmaceutical; D045304:Cytochromes c / Q000737:chemistry; D005990:Glycerol / Q000737:chemistry; D008956:Models, Chemical; D011489:Protein Denaturation; D017510:Protein Folding; D011506:Proteins / Q000737:chemistry*; D013816:Thermodynamics; D014867:Water / Q000737:chemistry
D011506:Proteins; C050095:zinc cytochrome c; D014867:Water; D045304:Cytochromes c; D005990:Glycerol