Evidence map›Paper›PMID 21911397›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2011

Signature of hydrophobic hydration in a single polymer.

Isaac T S Li, Gilbert C Walker

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
6.1field-weighted citation impact, top 3% of its field
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

33 citing papers in PubMed, 160 citations in OpenAlex.

  1. Article
  2. Extension of the molar absorption coefficient for non-ideal mixtures: an application to aqueous monovalent alcohol solutions.Analytical sciences : the international journal of the Japan Society for Analytical Chemistry · 2025
    Article
  3. Article
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  5. Review
  6. Article
  7. Orientational Preferences of GPI-Anchored Ly6/uPAR Proteins.International journal of molecular sciences · 2022
    Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Molecular Shape and the Hydrophobic Effect.Annual review of physical chemistry · 2016
    Review
  16. The hydrophobic effect, and fluctuations: The long and the short of it.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  17. Effects of Mutations on the Reconfiguration Rate of α-Synuclein.The journal of physical chemistry. B · 2015
    Article
  18. How osmolytes influence hydrophobic polymer conformations: A unified view from experiment and theory.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  19. Article
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

2 authors at 1 institution in 1 country.

Isaac T S LiDepartment of Chemistry, University of Toronto, 80 St George Street, Toronto, ON, Canada M5S 3H6.
Gilbert C Walker
University of Toronto · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Hydrophobicity underpins self-assembly in many natural and synthetic molecular and nanoscale systems. A signature of hydrophobicity is its temperature dependence. The first experimental evaluation of the temperature and size dependence of hydration free energy in a single hydrophobic polymer is reported, which tests key assumptions in models of hydrophobic interactions in protein folding. Herein, the hydration free energy required to extend three hydrophobic polymers with differently sized aromatic side chains was directly measured by single molecule force spectroscopy. The results are threefold. First, the hydration free energy per monomer is found to be strongly dependent on temperature and does not follow interfacial thermodynamics. Second, the temperature dependence profiles are distinct among the three hydrophobic polymers as a result of a hydrophobic size effect at the subnanometer scale. Third, the hydration free energy of a monomer on a macromolecule is different from a free monomer; corrections for the reduced hydration free energy due to hydrophobic interaction from neighboring units are required.

Indexed as

Hydrophobic and Hydrophilic InteractionsTemperatureModels, ChemicalPolymersSpectrum AnalysisThermodynamicsWaterPolymersWater

Identifiers

PMID21911397
PMCPMC3189081
OpenAlexW1998327691

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.