Evidence map›Paper›PMID 20385834›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2010

Why Hofmeister effects of many salts favor protein folding but not DNA helix formation.

Laurel M Pegram, Timothy Wendorff, Robert Erdmann, Irina Shkel, Dana Bellissimo, Daniel J Felitsky, M Thomas Record

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 65 papers.

0numbers the graph read from it
0cells of the map it votes in
65citing 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

65 citing papers in PubMed.

  1. Article
  2. Ion Adsorption at Surfaces from Local and Global Electroneutrality Constraints.Langmuir : the ACS journal of surfaces and colloids · 2026
    Article
  3. Article
  4. Article
  5. Article
  6. The Streptococcus phage protein paratox is an intrinsically disordered protein.Protein science : a publication of the Protein Society · 2024
    Article
  7. Article
  8. Article
  9. Salt Effects on Caffeine across Concentration Regimes.The journal of physical chemistry. B · 2023
    Article
  10. Structure and Formation of Z-DNA and Z-RNA.Molecules (Basel, Switzerland) · 2023
    Review
  11. Article
  12. Article
  13. Article
  14. Switchable DNA-Based Peroxidases Controlled by a Chaotropic Ion.Chembiochem : a European journal of chemical biology · 2022
    Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Review
  20. Article

5 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

7 authors.

Laurel M PegramDepartment of Biochemistry, University of Wisconsin-Madison, Madison, WI 53706, USA. Impegram@wisc.edu
Timothy Wendorff
Robert Erdmann
Irina Shkel
Dana Bellissimo
Daniel J Felitsky
M Thomas Record

Funding

THERMODYNAMIC AND NMR STUDIES ON THE E COLI CYTOPLASMR01GM047022 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI RECORD, M. THOMAS · 1992 to 2015
$4.1M
NIGMS NIH HHS GM47022NIGMS NIH HHS R01 GM047022
6 · The paper itself

Abstract

The majority ( approximately 70%) of surface buried in protein folding is hydrocarbon, whereas in DNA helix formation, the majority ( approximately 65%) of surface buried is relatively polar nitrogen and oxygen. Our previous quantification of salt exclusion from hydrocarbon (C) accessible surface area (ASA) and accumulation at amide nitrogen (N) and oxygen (O) ASA leads to a prediction of very different Hofmeister effects on processes that bury mostly polar (N, O) surface compared to the range of effects commonly observed for processes that bury mainly nonpolar (C) surface, e.g., micelle formation and protein folding. Here we quantify the effects of salts on folding of the monomeric DNA binding domain (DBD) of lac repressor (lac DBD) and on formation of an oligomeric DNA duplex. In accord with this prediction, no salt investigated has a stabilizing Hofmeister effect on DNA helix formation. Our ASA-based analyses of model compound data and estimates of the surface area buried in protein folding and DNA helix formation allow us to predict Hofmeister effects on these processes. We observe semiquantitative to quantitative agreement between these predictions and the experimental values, obtained from a novel separation of coulombic and Hofmeister effects. Possible explanations of deviations, including salt-dependent unfolded ensembles and interactions with other types of surface, are discussed.

Indexed as

Circular DichroismDNAHydrocarbonsLac RepressorsModels, ChemicalNitrogenNucleic Acid ConformationOxygenProtein FoldingSaltsThermodynamicsDNAHydrocarbonsLac RepressorsNitrogenOxygenSalts

Identifiers

PMID20385834
PMCPMC2867913

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.