Evidence map›Paper›PMID 25863066›Full record

ArticleBiophysical journal2015

Structural disorder of folded proteins: isotope-edited 2D IR spectroscopy and Markov state modeling.

Carlos R Baiz, Andrei Tokmakoff

Abstract read
In one paragraph

Article in Biophysical journal, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing 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

14 citing papers in PubMed.

  1. Article
  2. Article
  3. Modeling the Infrared Spectroscopy of Oligonucleotides withThe journal of physical chemistry. B · 2023
    Article
  4. AI-based spectroscopic monitoring of real-time interactions between SARS-CoV-2 and human ACE2.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Coordination to lanthanide ions distorts binding site conformation in calmodulin.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  10. Review
  11. Probing the Effects of Gating on the Ion Occupancy of the KJournal of the American Chemical Society · 2017
    Article
  12. Article
  13. Article
  14. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

2 authors.

Carlos R BaizDepartment of Chemistry, James Franck Institute and Institute for Biophysical Dynamics, The University of Chicago, Chicago, Illinois.
Andrei TokmakoffDepartment of Chemistry, James Franck Institute and Institute for Biophysical Dynamics, The University of Chicago, Chicago, Illinois. Electronic address: tokmakoff@uchicago.edu.

Funding

Wide-Field Short-Wave Infrared (SWIR) multiphoton (MP) tissue imagingP41EB015871 · NIBIB · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI SO, PETER T. · 2012 to 2021
$11.3M
Developing a spectroscopic toolkit for probing protein structure and foldingF32GM105104 · NIGMS · UNIVERSITY OF CHICAGO · PI BAIZ, CARLOS RAUL · 2013 to 2014
$102k
NIBIB NIH HHS P41 EB015871NIGMS NIH HHS F32 GM105104NIGMS NIH HHS F32GM105104
6 · The paper itself

Abstract

The conformational heterogeneity of the N-terminal domain of the ribosomal protein L9 (NTL91-39) in its folded state is investigated using isotope-edited two-dimensional infrared spectroscopy. Backbone carbonyls are isotope-labeled ((13)C=(18)O) at five selected positions (V3, V9, V9G13, G16, and G24) to provide a set of localized spectroscopic probes of the structure and solvent exposure at these positions. Structural interpretation of the amide I line shapes is enabled by spectral simulations carried out on structures extracted from a recent Markov state model. The V3 label spectrum indicates that the β-sheet contacts between strands I and II are well folded with minimal disorder. The V9 and V9G13 label spectra, which directly probe the hydrogen-bond contacts across the β-turn, show significant disorder, indicating that molecular dynamics simulations tend to overstabilize ideally folded β-turn structures in NTL91-39. In addition, G24-label spectra provide evidence for a partially disordered α-helix backbone that participates in hydrogen bonding with the surrounding water.

Indexed as

Molecular Dynamics SimulationProtein FoldingAmino Acid MotifsAmino Acid SequenceMolecular Sequence DataProtein Structure, TertiaryRibosomal Proteinsribosomal protein L9Ribosomal Proteins

Identifiers

PMID25863066
PMCPMC4390782

What OpenQuestion holds

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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.