Evidence map›Paper›PMID 17993487›Full record

ArticleBiophysical journal2008

Stochastic study of the effect of ionic strength on noncovalent interactions in protein pores.

Qitao Zhao, Dilani A Jayawardhana, Xiyun Guan

Open access · hybridAbstract read
In one paragraph

Article in Biophysical journal, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
2.7field-weighted citation impact, top 11% 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

21 citing papers in PubMed, 46 citations in OpenAlex.

  1. Article
  2. Review
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  4. Probe-assisted detection of FeBiosensors & bioelectronics · 2024
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  10. Salt-Mediated Nanopore Detection of ADAM-17.ACS applied bio materials · 2019
    Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Unzipping of Double-stranded DNA in Engineered α-Hemolysin Pores.The journal of physical chemistry letters · 2011
    Article
  20. Article
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

3 authors at 1 institution in 1 country.

Qitao ZhaoDepartment of Chemistry and Biochemistry, The University of Texas at Arlington, Arlington, Texas 76019-0065, USA.
Dilani A Jayawardhana
Xiyun Guan
The University of Texas at Arlington · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Salt plays a critical role in the physiological activities of cells. We show that ionic strength significantly affects the kinetics of noncovalent interactions in protein channels, as observed in stochastic studies of the transfer of various analytes through pores of wild-type and mutant alpha-hemolysin proteins. As the ionic strength increased, the association rate constant of electrostatic interactions was accelerated, whereas those of both hydrophobic and aromatic interactions were retarded. Dramatic decreases in the dissociation rate constants, and thus increases in the overall reaction formation constants, were observed for all noncovalent interactions studied. The results suggest that with the increase of salt concentration, the streaming potentials for all the protein pores decrease, whereas the preferential selectivities of the pores for either cations or anions drop. Furthermore, results also show that the salt effect on the rate of association of analytes to a pore differs significantly depending on the nature of the noncovalent interactions occurring in the protein channel. In addition to providing new insights into the nature of analyte-protein pore interactions, the salt-dependence of noncovalent interactions in protein pores observed provides a useful means to greatly enhance the sensitivity of the nanopore, which may find useful application in stochastic sensing.

Indexed as

Ion Channel GatingModels, ChemicalModels, MolecularBinding SitesComputer SimulationHydrogen-Ion ConcentrationIon ChannelsIonsProtein BindingProtein ConformationProtein Interaction MappingProteinsStochastic ProcessesIon ChannelsIonsProteins

Identifiers

PMID17993487
PMCPMC2212693
OpenAlexW2051395053

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.