Evidence map›Paper›PMID 21683504›Full record

ArticleBiophysical chemistry2011

Osmolyte effects on protein stability and solubility: a balancing act between backbone and side-chains.

Matthew Auton, Jörg Rösgen, Mikhail Sinev, Luis Marcelo F Holthauzen, D Wayne Bolen

Abstract read
In one paragraph

Article in Biophysical chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 98 papers.

0numbers the graph read from it
0cells of the map it votes in
98citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

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

98 citing papers in PubMed.

  1. Article
  2. First Hydration Shell Integrity: Key to Protein Stability.Journal of the American Chemical Society · 2026
    Article
  3. Article
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  6. Article
  7. Review
  8. Review
  9. Article
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  11. Article
  12. Article
  13. Review
  14. Article
  15. Trimethylamine-N-oxide depletes urea in a peptide solvation shell.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  16. Review
  17. Article
  18. Article
  19. Article
  20. Review

38 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors.

Matthew AutonDepartment of Medicine, Cardiovascular Research, Baylor College of Medicine, Houston, TX, United States.
Jörg Rösgen
Mikhail Sinev
Luis Marcelo F Holthauzen
D Wayne Bolen

Funding

Osmolytes on protein structure and energeticsR01GM049760 · NIGMS · UNIVERSITY OF TEXAS MEDICAL BR GALVESTON · PI ROSGEN, JORG · 1993 to 2014
$4.3M
NIGMS NIH HHS GM049760NIGMS NIH HHS R01 GM049760
6 · The paper itself

Abstract

In adaptation biology the discovery of intracellular osmolyte molecules that in some cases reach molar levels, raises questions of how they influence protein thermodynamics. We've addressed such questions using the premise that from atomic coordinates, the transfer free energy of a native protein (ΔG(tr,N)) can be predicted by summing measured water-to-osmolyte transfer free energies of the protein's solvent exposed side chain and backbone component parts. ΔG(tr,D) is predicted using a self avoiding random coil model for the protein, and ΔG(tr,D)-ΔG(tr,N), predicts the m-value, a quantity that measures the osmolyte effect on the N⇌D transition. Using literature and newly measured m-values we show 1:1 correspondence between predicted and measured m-values covering a range of 12 kcal/mol/M in protein stability for 46 proteins and 9 different osmolytes. Osmolytes present a range of side chain and backbone effects on N and D solubility and protein stability key to their biological roles.

Indexed as

BetaineGlycerolModels, BiologicalOsmolar ConcentrationProlineProteinsProtein StabilitySolubilityUreaBetaineGlycerolProlineProteinsUrea

Identifiers

PMID21683504
PMCPMC3166983

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Registered trials

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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.