Evidence map›Paper›PMID 17031938›Full record

ArticleJournal of the American Chemical Society2006

Site-specific conversion of cysteine thiols into thiocyanate creates an IR probe for electric fields in proteins.

Aaron T Fafarman, Lauren J Webb, Jessica I Chuang, Steven G Boxer

Open access · greenAbstract read
In one paragraph

Article in Journal of the American Chemical Society, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 76 papers.

0numbers the graph read from it
0cells of the map it votes in
76citing papers in PubMed
2.9field-weighted citation impact, top 10% 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

76 citing papers in PubMed, 210 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Review
  7. Increasing Pump-Probe Signal toward Asymptotic Limits.The journal of physical chemistry. B · 2023
    Review
  8. Article
  9. Article
  10. Review
  11. Versatile Vibrational Energy Sensors for Proteins.Angewandte Chemie (International ed. in English) · 2022
    Article
  12. Article
  13. Article
  14. TfNNACS omega · 2022
    Article
  15. Site-Specific Interrogation of Protein Structure and Stability.Methods in molecular biology (Clifton, N.J.) · 2022
    Article
  16. Transparent window 2D IR spectroscopy of proteins.The Journal of chemical physics · 2021
    Review
  17. Protein Dynamics by Two-Dimensional Infrared Spectroscopy.Annual review of analytical chemistry (Palo Alto, Calif.) · 2021
    Article
  18. Extending the vibrational lifetime of azides with heavy atoms.Physical chemistry chemical physics : PCCP · 2020
    Article
  19. Article
  20. Article

16 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

4 authors at 1 institution in 1 country.

Aaron T FafarmanDepartment of Chemistry, Stanford University, Stanford, CA 94305-5080, USA.
Lauren J Webb
Jessica I Chuang
Steven G Boxer
Stanford University · US

Funding

ELECTROSTATICS AND DYNAMICS IN MYOGLOBIN MUTANTSR37GM027738 · NIGMS · STANFORD UNIVERSITY · PI BOXER, STEVEN G. · 1994 to 2003
$1.2M
Vibrational Stark Effect in Human Aldose ReductaseF32GM076833 · NIGMS · STANFORD UNIVERSITY · PI WEBB, LAUREN J · 2006 to 2008
$117k
NIGMS NIH HHS F32 GM076833NIGMS NIH HHS R37 GM027738
6 · The paper itself

Abstract

The nitrile stretching mode of the thiocyanate moiety is a nearly ideal probe for measuring the local electric field arising from the organized environment of the interior of a protein. Nitriles were introduced into three proteins: ribonuclease S (RNase S), human aldose reductase (hALR2), and the reaction center (RC) of Rhodobacter capsulatus, through a facile synthetic scheme for the transformation of cysteine residues into thiocyanatoalanine. Vibrational Stark effect spectroscopy and Fourier transform infrared spectroscopy on the modified proteins demonstrated that thiocyanate residues are a highly general tool for probing electrostatic fields in proteins.

Indexed as

CysteineElectromagnetic FieldsProtein EngineeringProteinsSpectrophotometry, InfraredStatic ElectricitySulfhydryl CompoundsTemperatureThiocyanatesCysteineProteinsSulfhydryl CompoundsthiocyanateThiocyanates

Identifiers

PMID17031938
PMCPMC2516909
OpenAlexW2071558544

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.