Evidence map›Paper›PMID 21219136›Full record

ReviewAnnual review of physical chemistry2011

Role of solvation effects in protein denaturation: from thermodynamics to single molecules and back.

Jeremy L England, Gilad Haran

Open access · greenAbstract readReview
In one paragraph

Review in Annual review of physical chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 83 papers.

0numbers the graph read from it
0cells of the map it votes in
83citing papers in PubMed
11.2field-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

83 citing papers in PubMed, 274 citations in OpenAlex.

  1. Article
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  5. Implicit Solvent Sample-Based Quantum Diagonalization.The journal of physical chemistry. B · 2025
    Article
  6. Strong adsorption of guanidinium cations to the air-water interface.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  7. Article
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  12. Article
  13. ACS applied materials & interfaces · 2023
    Article
  14. Article
  15. Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article

23 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

2 authors at 2 institutions in 2 countries.

Jeremy L EnglandLewis-Sigler Institute for Integrative Genomics, Princeton University, Princeton, New Jersey 08544, USA.
Gilad Haran
Princeton University · USWeizmann Institute of Science · IL

Funding

Single-molecule fluorescence studies of protein foldingR01GM080515 · NIGMS · WEIZMANN INSTITUTE OF SCIENCE · PI HARAN, GILAD · 2007 to 2010
$992k
NIGMS NIH HHS R01 GM080515NIGMS NIH HHS R01GM080515
6 · The paper itself

Abstract

Protein stability often is studied in vitro through the use of urea and guanidinium chloride, chemical cosolvents that disrupt protein native structure. Much controversy still surrounds the underlying mechanism by which these molecules denature proteins. Here we review current thinking on various aspects of chemical denaturation. We begin by discussing classic models of protein folding and how the effects of denaturants may fit into this picture through their modulation of the collapse, or coil-globule transition, which typically precedes folding. Subsequently, we examine recent molecular dynamics simulations that have shed new light on the possible microscopic origins of the solvation effects brought on by denaturants. It seems likely that both denaturants operate by facilitating solvation of hydrophobic regions of proteins. Finally, we present recent single-molecule fluorescence studies of denatured proteins, the analysis of which corroborates the role of denaturants in shifting the equilibrium of the coil-globule transition.

Indexed as

Molecular Dynamics SimulationThermodynamicsFluorescence Resonance Energy TransferGuanidineHydrophobic and Hydrophilic InteractionsProtein ConformationProtein DenaturationProtein FoldingProteinsProtein Structure, SecondarySolventsUreaWaterGuanidineProteinsSolventsUreaWater

Identifiers

PMID21219136
PMCPMC3211090
OpenAlexW2103751982

What OpenQuestion holds

Textmetadata
LicenceTDM
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.