Evidence map›Paper›PMID 23394622›Full record

ArticleJournal of the American Chemical Society2013

Chiral sum frequency generation for in situ probing proton exchange in antiparallel β-sheets at interfaces.

Li Fu, Dequan Xiao, Zhuguang Wang, Victor S Batista, Elsa C Y Yan

Abstract read
In one paragraph

Article in Journal of the American Chemical Society, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing 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

19 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Mirror-image antiparallel β-sheets organize water molecules into superstructures of opposite chirality.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  7. Article
  8. Article
  9. Article
  10. Observation of pH-Induced Protein Reorientation at the Water Surface.The journal of physical chemistry letters · 2017
    Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Theoretical Sum Frequency Generation Spectroscopy of Peptides.The journal of physical chemistry. B · 2015
    Article
  16. Article
  17. Article
  18. Article
  19. 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

5 authors.

Li FuDepartment of Chemistry, Yale University, 225 Prospect Street, New Haven, Connecticut 06520, United States.
Dequan Xiao
Zhuguang Wang
Victor S Batista
Elsa C Y Yan

Funding

ELECTRONIC STRUCTURE OF FE-OXO AND MN-OXO COMPLEXESR01GM043278 · NIGMS · SCRIPPS RESEARCH INSTITUTE, THE · PI NOODLEMAN, LOUIS · 1991 to 2010
$2.7M
Studies of redox-active sites in Photosystem IIR01GM084267 · NIGMS · YALE UNIVERSITY · PI BATISTA, VICTOR S · 2009 to 2010
$395k
NIGMS NIH HHS 1R01 GM-084267-01NIGMS NIH HHS GM-043278NIGMS NIH HHS R01 GM043278NIGMS NIH HHS R01 GM084267
6 · The paper itself

Abstract

Studying hydrogen/deuterium (H/D) exchange in proteins can provide valuable insight on protein structure and dynamics. Several techniques are available for probing H/D exchange in the bulk solution, including NMR, mass spectroscopy, and Fourier transform infrared spectroscopy. However, probing H/D exchange at interfaces is challenging because it requires surface-selective methods. Here, we introduce the combination of in situ chiral sum frequency generation (cSFG) spectroscopy and ab initio simulations of cSFG spectra as a powerful methodology to probe the dynamics of H/D exchange at interfaces. This method is applied to characterize H/D exchange in the antiparallel β-sheet peptide LK7β. We report here for the first time that the rate of D-to-H exchange is about 1 order of magnitude faster than H-to-D exchange in the antiparallel structure at the air/water interface, which is consistent with the existing knowledge that O-H/D dissociation in water is the rate-limiting step, and breaking the O-D bond is slower than breaking the O-H bond. The reported analysis also provides fundamental understanding of several vibrational modes and their couplings in peptide backbones that have been difficult to characterize by conventional methods, including Fermi resonances of various combinations of peptide vibrational modes such as amide I and amide II, C-N stretch, and N-H/N-D bending. These results demonstrate cSFG as a sensitive technique for probing the kinetics of H/D exchange in proteins at interfaces, with high signal-to-noise N-H/N-D stretch bands that are free of background from the water O-H/O-D stretch.

Indexed as

ProtonsDeuterium Exchange MeasurementPeptidesProtein Structure, SecondaryQuantum TheorySpectrum AnalysisPeptidesProtons

Identifiers

PMID23394622
PMCPMC9208335

What OpenQuestion holds

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Registered trials

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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.