Evidence map›Paper›PMID 16505377›Full record

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

Picosecond dynamics of a membrane protein revealed by 2D IR.

Prabuddha Mukherjee, Itamar Kass, Isaiah T Arkin, Isaiah Arkin, Martin T Zanni

Erratum issuedAbstract 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. An erratum has been issued. Cited by 63 papers.

0numbers the graph read from it
0cells of the map it votes in
63citing 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

63 citing papers in PubMed.

  1. Do selectivity filter carbonyls in KJournal of structural biology: X · 2024
    Article
  2. Water inside the Selectivity Filter of a KJournal of the American Chemical Society · 2024
    Article
  3. Article
  4. Protein Dynamics by Two-Dimensional Infrared Spectroscopy.Annual review of analytical chemistry (Palo Alto, Calif.) · 2021
    Article
  5. Article
  6. Ultrafast Dynamics at Lipid-Water Interfaces.Accounts of chemical research · 2020
    Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Theoretical Sum Frequency Generation Spectroscopy of Peptides.The journal of physical chemistry. B · 2015
    Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article

3 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

  • Erratum issued
    Arkin, Isaiah [corrected to Arkin, Isaiah T]
5 · Who and what money

Authors and funding

5 authors.

Prabuddha MukherjeeDepartment of Chemistry, University of Wisconsin, Madison, WI 53706-1396, USA.
Itamar Kass
Isaiah T Arkin
Isaiah Arkin
Martin T Zanni

Funding

1 and 2D IR structural analyses of Influenza M2 channelR21AI064797 · NIAID · UNIVERSITY OF WISCONSIN-MADISON · PI ZANNI, MARTIN T · 2005 to 2006
$492k
NIAID NIH HHS 1R21AI064797-01NIAID NIH HHS R21 AI064797
6 · The paper itself

Abstract

Fast protein dynamics can be missed with techniques that have relatively slow observation times. Using 2D IR spectroscopy and isotope labeling, we have probed the rapid, picosecond dynamics of a membrane protein in its native environment. By measuring the homogeneous and inhomogeneous IR linewidths of 11 amide I modes (backbone carbonyl stretch), we have captured the structural distributions and dynamics of the CD3zeta protein along its transmembrane segment that are lost with slower time-scale techniques. We find that the homogeneous lifetimes and population relaxation times are the same for almost all of the residues. In contrast, the inhomogeneous linewidths vary significantly with the largest inhomogeneous distribution occurring for residues near the N terminus and the narrowest near the center. This behavior is highly consistent with a recently reported experimental model of the protein and water accessibility as observed by molecular dynamics simulations. The data support the proposed CD3zeta peptide structure, and the simulations point to the structural disorder of water and lipid head-groups as the main source of inhomogeneous broadening. Taken together, this rigorous analysis of the vibrational dynamics of a membrane peptide provides experimental insight into a time regime of motions that has so far been largely unexplored.

Indexed as

CD3 ComplexComputer SimulationHumansMembrane LipidsMembrane ProteinsModels, MolecularProtein Structure, SecondarySpectrophotometry, InfraredThermodynamicsWaterCD3 antigen, zeta chainCD3 ComplexMembrane LipidsMembrane ProteinsWater

Identifiers

PMID16505377
PMCPMC1383493

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.