Evidence map›Paper›PMID 21987795›Full record

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

Extended surfaces modulate hydrophobic interactions of neighboring solutes.

Amish J Patel, Patrick Varilly, Sumanth N Jamadagni, Hari Acharya, Shekhar Garde, David Chandler

Open access · greenAbstract 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 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed
10.6field-weighted citation impact, top 1% 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

38 citing papers in PubMed, 165 citations in OpenAlex.

  1. Article
  2. Article
  3. Understanding Sorption Mechanisms Directly from Isotherms.Langmuir : the ACS journal of surfaces and colloids · 2023
    Article
  4. Article
  5. Article
  6. Learning the relationship between nanoscale chemical patterning and hydrophobicity.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  7. Review
  8. Article
  9. Article
  10. Size dependence of hydrophobic hydration at electrified gold/water interfaces.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  11. Affinity of small-molecule solutes to hydrophobic, hydrophilic, and chemically patterned interfaces in aqueous solution.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  12. Article
  13. Light-induced dilation in nanosheets of charge-transfer complexes.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  14. Hydrophobicity of proteins and nanostructured solutes is governed by topographical and chemical context.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Review
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

6 authors at 3 institutions in 1 country.

Amish J PatelHoward P Isermann Department of Chemical and Biological Engineering, and Center for Biotechnology and Interdisciplinary Studies, Rensselaer Polytechnic Institute, Troy, NY 12180, USA.
Patrick Varilly
Sumanth N Jamadagni
Hari Acharya
Shekhar Garde
David Chandler
Rensselaer Polytechnic Institute · USUniversity of California, Berkeley · USProcter & Gamble (United States) · US

Funding

Hydrophobic Effects in Biophysical Systems and Protein-Protein InteractionsR01GM078102 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI CHANDLER, DAVID · 2007 to 2010
$897k
NIGMS NIH HHS R01 GM078102NIGMS NIH HHS R01-GM078102-04
6 · The paper itself

Abstract

Interfaces are a most common motif in complex systems. To understand how the presence of interfaces affects hydrophobic phenomena, we use molecular simulations and theory to study hydration of solutes at interfaces. The solutes range in size from subnanometer to a few nanometers. The interfaces are self-assembled monolayers with a range of chemistries, from hydrophilic to hydrophobic. We show that the driving force for assembly in the vicinity of a hydrophobic surface is weaker than that in bulk water and decreases with increasing temperature, in contrast to that in the bulk. We explain these distinct features in terms of an interplay between interfacial fluctuations and excluded volume effects--the physics encoded in Lum-Chandler-Weeks theory [Lum K, Chandler D, Weeks JD (1999) J Phys Chem B 103:4570-4577]. Our results suggest a catalytic role for hydrophobic interfaces in the unfolding of proteins, for example, in the interior of chaperonins and in amyloid formation.

Indexed as

Hydrophobic and Hydrophilic InteractionsModels, ChemicalMolecular Dynamics SimulationProteinsSolutionsSurface PropertiesTemperatureThermodynamicsWaterProteinsSolutionsWater

Identifiers

PMID21987795
PMCPMC3203787
OpenAlexW1969893670

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.