Protein phase diagrams: The physics behind their elliptic shape

Lesch, H.; Hecht, C.; Friedrich, J.

doi:10.1063/1.1824900

Cited by 20 publications

(31 citation statements)

References 28 publications

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“…Although we interpret the elliptic phase boundary as a special feature of a general property of proteins (33), namely their intrinsic disorder and the resulting low correlation between enthalpy and volume fluctuations, the implications are severe: for the ellipse condition to generally hold true (Eq. 6), the changes in compressibility ⌬␤ and in the specific heat ⌬C p are bound to have the same sign.…”

Section: [1]mentioning

confidence: 99%

Temperature and pressure dependence of protein stability: The engineered fluorescein-binding lipocalin FluA shows an elliptic phase diagram

Wiedersich

Köhler

Skerra

et al. 2008

Proc. Natl. Acad. Sci. U.S.A.

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We have measured the equilibrium constant for the denaturation transition of the engineered fluorescein-binding lipocalin FluA as a function of pressure and temperature, taking advantage of the fact that the ligand's fluorescence is almost fully quenched when complexed with the folded protein, but reversibly reappears on denaturation. From the equilibrium constant as a function of pressure and temperature all of the involved thermodynamic parameters of protein folding, in particular the changes in entropy and volume, compressibility, thermal expansion, and specific heat, were deduced in a global fitting procedure. Assuming that these parameters are independent of temperature and pressure, we can demonstrate from the ratio of ⌬␤, ⌬␣ 2 , ⌬Cp that the phase diagram of protein folding assumes an elliptic shape. Furthermore, we can show that the thermodynamic condition for such an elliptic phase diagram is related to the degree of correlation between the fluctuations of the changes in volume and enthalpy at the phase boundary. For the protein investigated this correlation is low, as generally expected for highly degenerate systems. Our study suggests that the elliptic phase diagram is a consequence of the inherent conformational disorder of proteins and that it may be viewed as the thermodynamic manifestation of the high degeneracy of conformational energies that is characteristic for this class of macromolecules.anticalin ͉ denaturation ͉ engineering ͉ folding ͉ thermodynamics

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Section: [1]mentioning

confidence: 99%

Temperature and pressure dependence of protein stability: The engineered fluorescein-binding lipocalin FluA shows an elliptic phase diagram

Wiedersich

Köhler

Skerra

et al. 2008

Proc. Natl. Acad. Sci. U.S.A.

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“…The mathematical implications and assumptions that are usually made in the analysis of the data have been recently discussed (14). The physics behind the elliptic phase diagram can be related to the degree of correlation between the enthalpy and volume change of the unfolding transition (15).…”

Section: The Stability Diagram: Thermodynamic Aspectsmentioning

confidence: 99%

Protein dynamics: hydration and cavities

Heremans

2005

Braz J Med Biol Res

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The temperature-pressure behavior of proteins seems to be unique among the biological macromolecules. Thermodynamic as well as kinetic data show the typical elliptical stability diagram. This may be extended by assuming that the unfolded state gives rise to volume and enthalpy-driven liquid-liquid transitions. A molecular interpretation follows from the temperature and the pressure dependence of the hydration and cavities. We suggest that positron annihilation spectroscopy can provide additional quantitative evidence for the contributions of cavities to the dynamics of proteins. Only mature amyloid fibrils that form from unfolded proteins are very resistant to pressure treatment.

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“…(7a) to data reported by Lesch and co-workers for a protein of Zn-Cytochrome c [12,13]. In order to obtain directly the minimum temperature T 1 and the maximum temperature T 2 , it is preferable to write the Eq.…”

Section: -Application To the P-t Elliptic Phase Diagram Of Proteinmentioning

confidence: 99%

“…If C P is constant as supposed in all the previous studies [12,13] and since the  (  ) , then the enthalpy must be a linear function of T, which is incompatible with the P-T phase diagram of elliptical shape.…”

Section: -Introductionmentioning

confidence: 99%

Thermodynamics of protein unfolding-refolding transition

Jeanfils¹,

Anakkar²,

Jean-Marc³

2014

Int. J. Thermo

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A phenomenological thermodynamic model is developed to investigate, in more detail than usual, the pressuretemperature phase diagram of proteins. Indeed, in the whole of previous studies the specific heat difference C P is treated as pressure and temperature independent. This assumption is wrong, as confirmed by Yamaguchi et al [1] which reported pressure dependence of C P in the case of ribonuclease A. In this work, assuming that the chemical potential has a Taylor series expansion and having an additional thermodynamic piece of information, the analysis shows that it is possible to obtain a complete description of the unfolding-refolding transition of protein, to deduce the volumes, entropies, enthalpies versus transition temperatures and transition pressures and, for the first time, to deduce the specific heat changes versus transition temperatures and transition pressures. Special attention is given to the elliptical shape of the pressure-temperature phase diagram. A quantitative description of the phase transitions in the protein of Zn-Cytochrome c is given.

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Protein phase diagrams: The physics behind their elliptic shape

Cited by 20 publications

References 28 publications

Temperature and pressure dependence of protein stability: The engineered fluorescein-binding lipocalin FluA shows an elliptic phase diagram

Temperature and pressure dependence of protein stability: The engineered fluorescein-binding lipocalin FluA shows an elliptic phase diagram

Protein dynamics: hydration and cavities

Thermodynamics of protein unfolding-refolding transition

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