Evidence map›Paper›PMID 21636774›Full record

ArticleScience (New York, N.Y.)2011

Residue-specific vibrational echoes yield 3D structures of a transmembrane helix dimer.

Amanda Remorino, Ivan V Korendovych, Yibing Wu, William F DeGrado, Robin M Hochstrasser

Abstract read
In one paragraph

Article in Science (New York, N.Y.), 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed
9.7field-weighted citation impact, top 1% 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

38 citing papers in PubMed, 104 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Review
  10. Computing infrared spectra of proteins using the exciton model.Journal of computational chemistry · 2017
    Article
  11. Simple method to introduce an ester infrared probe into proteins.Protein science : a publication of the Protein Society · 2017
    Article
  12. Minimalist IR and fluorescence probes of protein function.Current opinion in chemical biology · 2016
    Review
  13. Article
  14. Review
  15. Article
  16. How Sensitive is the Amide I Vibration of the Polypeptide Backbone to Electric Fields?Chemphyschem : a European journal of chemical physics and physical chemistry · 2015
    Article
  17. Review
  18. Review
  19. Line shape analysis of two-dimensional infrared spectra.The Journal of chemical physics · 2015
    Article
  20. Site-specific infrared probes of proteins.Annual review of physical chemistry · 2015
    Review
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 at 1 institution in 1 country.

Amanda RemorinoDepartment of Chemistry, University of Pennsylvania, Philadelphia, PA 19104-6323, USA.
Ivan V Korendovych
Yibing Wu
William F DeGrado
Robin M Hochstrasser
University of Pennsylvania · US

Funding

ZN-INDUCED PEPTIDE FOLDINGP41RR001348 · NCRR · UNIVERSITY OF PENNSYLVANIA · PI DEGRADO, WILLIAM · 1985 to 2011
$8.7M
Structure of M2 Proton Channel from Influenza A VirusR01GM056423 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI DEGRADO, WILLIAM · 1997 to 2016
$4.5M
De novo design of alpha-helical bundlesR37GM054616 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI DEGRADO, WILLIAM · 2004 to 2013
$3.6M
Ultrafast Processing in Proteins and Other AssembliesR01GM012592 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI GAI, FENG · 1985 to 2013
$3.5M
DE NOVO DESIGN OF ALPHA HELICAL BUNDLESR01GM054616 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI DEGRADO, WILLIAM · 1996 to 2016
$2.4M
BIOORGANIC MODELS FOR TRANSMEMBRANE PROTEINSR01GM060610 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI DEGRADO, WILLIAM · 2000 to 2009
$2.2M
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 RR01348NIGMS NIH HHS GM12592NIGMS NIH HHS GM54616NIGMS NIH HHS GM56423NIGMS NIH HHS GM60610NIGMS NIH HHS R01 GM012592NIGMS NIH HHS R01 GM054616NIGMS NIH HHS R01 GM056423NIGMS NIH HHS R37 GM012592NIGMS NIH HHS R37 GM054616
6 · The paper itself

Abstract

Two-dimensional (2D) vibrational echo spectroscopy has previously been applied to structural determination of small peptides. Here we extend the technique to a more complex, biologically important system: the homodimeric transmembrane dimer from the α chain of the integrin α(IIb)β(3). We prepared micelle suspensions of the pair of 30-residue chains that span the membrane in the native structure, with varying levels of heavy ((13)C=(18)O) isotopes substituted in the backbone of the central 10th through 20th positions. The constraints derived from vibrational coupling of the precisely spaced heavy residues led to determination of an optimized structure from a range of model candidates: Glycine residues at the 12th, 15th, and 16th positions form a tertiary contact in parallel right-handed helix dimers with crossing angles of -58° ± 9° and interhelical distances of 7.7 ± 0.5 angstroms. The frequency correlation established the dynamical model used in the analysis, and it indicated the absence of mobile water associated with labeled residues. Delocalization of vibrational excitations between the helices was also quantitatively established.

Indexed as

Amino Acid MotifsCarbon IsotopesCell MembraneEnergy TransferMicellesModels, MolecularMolecular Dynamics SimulationOxygen IsotopesPeptidesPlatelet Membrane Glycoprotein IIbProtein MultimerizationProtein Structure, SecondaryProtein Structure, TertiarySpectrophotometry, InfraredSpectroscopy, Fourier Transform InfraredVibrationCarbon IsotopesMicellesOxygen IsotopesPeptidesPlatelet Membrane Glycoprotein IIb

Identifiers

PMID21636774
PMCPMC3295544
OpenAlexW2095022530

What OpenQuestion holds

Textmetadata
LicenceTDM
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.