Evidence map›Paper›PMID 18391216›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2008

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

Johannes Wiedersich, Simone Köhler, Arne Skerra, Josef Friedrich

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

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Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

13 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
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  6. Article
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  8. Article
  9. Effects of pressure and temperature on the binding of RecA protein to single-stranded DNA.Proceedings of the National Academy of Sciences of the United States of America · 2011
    Article
  10. Article
  11. Article
  12. Computing the stability diagram of the Trp-cage miniprotein.Proceedings of the National Academy of Sciences of the United States of America · 2008
    Article
  13. Why elliptical stability diagrams are not related to protein conformational disorder.Proceedings of the National Academy of Sciences of the United States of America · 2008
    Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

4 authors.

Johannes WiedersichLehrstuhl für Physik Weihenstephan, Technische Universität München, 85350 Freising, Germany.
Simone Köhler
Arne Skerra
Josef Friedrich

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

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 Deltabeta, Deltaalpha(2), DeltaC(p) 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.

Indexed as

Phase TransitionPressureTemperatureThermodynamicsFluoresceinLipocalinsProtein DenaturationProtein FoldingProteinsRecombinant ProteinsFluoresceinlipocalin FluALipocalinsProteinsRecombinant Proteins

Identifiers

PMID18391216
PMCPMC2311345

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.