Evidence map›Paper›PMID 17075037›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2006

Amide vibrations are delocalized across the hydrophobic interface of a transmembrane helix dimer.

Chong Fang, Alessandro Senes, Lidia Cristian, William F DeGrado, Robin M Hochstrasser

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing 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

22 citing papers in PubMed.

  1. Article
  2. Article
  3. Protein Dynamics by Two-Dimensional Infrared Spectroscopy.Annual review of analytical chemistry (Palo Alto, Calif.) · 2021
    Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Discovery of competing anaerobic and aerobic pathways in umpolung amide synthesis allows for site-selective amide 18O-labeling.Proceedings of the National Academy of Sciences of the United States of America · 2012
    Article
  11. Article
  12. Article
  13. Tidal surge in the M2 proton channel, sensed by 2D IR spectroscopy.Proceedings of the National Academy of Sciences of the United States of America · 2011
    Article
  14. Article
  15. 2D IR provides evidence for mobile water molecules in beta-amyloid fibrils.Proceedings of the National Academy of Sciences of the United States of America · 2009
    Article
  16. Article
  17. Article
  18. Article
  19. Review
  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

5 authors.

Chong FangDepartment of Chemistry, University of Pennsylvania, Philadelphia, PA 19104-6323, USA.
Alessandro Senes
Lidia Cristian
William F DeGrado
Robin M Hochstrasser

Funding

ZN-INDUCED PEPTIDE FOLDINGP41RR001348 · NCRR · UNIVERSITY OF PENNSYLVANIA · PI DEGRADO, WILLIAM · 1985 to 2011
$8.7M
Vibrational and Optical Probes of Electric Fields in ProteinsP01GM048130 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI HOCHSTRASSER, ROBIN MAIN · 1993 to 2007
$7.3M
Ultrafast Processing in Proteins and Other AssembliesR01GM012592 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI GAI, FENG · 1985 to 2013
$3.5M
ULTRAFAST PROCESSES IN PROTEINS AND OTHER ASSEMBLIESR37GM012592 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI HOCHSTRASSER, ROBIN MAIN · 1992 to 2001
$493k
NCRR NIH HHS P41 RR001348NCRR NIH HHS RR 001348NIGMS NIH HHS 5P01 GM 48130NIGMS NIH HHS GM 12592NIGMS NIH HHS P01 GM048130NIGMS NIH HHS R01 GM012592NIGMS NIH HHS R37 GM012592
6 · The paper itself

Abstract

The tertiary interactions between amide-I vibrators on the separate helices of transmembrane helix dimers were probed by ultrafast 2D vibrational photon echo spectroscopy. The 2D IR approach proves to be a useful structural method for the study of membrane-bound structures. The 27-residue human erythrocyte protein Glycophorin A transmembrane peptide sequence: KKITLIIFG(79)VMAGVIGTILLISWG(94)IKK was labeled at G(79) and G(94) with (13)C=(16)O or (13)C=(18)O. The isotopomers and their 50:50 mixtures formed helical dimers in SDS micelles whose 2D IR spectra showed components from homodimers when both helices had either (13)C=(16)O or (13)C=(18)O substitution and a heterodimer when one had (13)C=(16)O substitution and the other had (13)C=(18)O substitution. The cross-peaks in the pure heterodimer 2D IR difference spectrum and the splitting of the homodimer peaks in the linear IR spectrum show that the amide-I mode is delocalized across a pair of helices. The excitation exchange coupling in the range 4.3-6.3 cm(-1) arises from through-space interactions between amide units on different helices. The angle between the two Gly(79) amide-I transition dipoles, estimated at 103 degrees from linear IR spectroscopy and 110 degrees from 2D IR spectroscopy, combined with the coupling led to a structural picture of the hydrophobic interface that is remarkably consistent with results from NMR on helix dimers. The helix crossing angle in SDS is estimated at 45 degrees. Two-dimensional IR spectroscopy also sets limits on the range of geometrical parameters for the helix dimers from an analysis of the coupling constant distribution.

Indexed as

AmidesAmino Acid SequenceBiophysical PhenomenaBiophysicsDimerizationGlycophorinsHumansHydrophobic and Hydrophilic InteractionsIn Vitro TechniquesMembrane ProteinsModels, MolecularMolecular Sequence DataPeptide FragmentsProtein Structure, QuaternaryProtein Structure, SecondarySpectroscopy, Fourier Transform InfraredAmidesGlycophorinsMembrane ProteinsPeptide Fragments

Identifiers

PMID17075037
PMCPMC1636525

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.