Evidence map›Paper›PMID 28461483›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2017

Efficient assignment and NMR analysis of an intact virus using sequential side-chain correlations and DNP sensitization.

Ivan V Sergeyev, Boris Itin, Rivkah Rogawski, Loren A Day, Ann E McDermott

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing 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

37 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Resolution in cryogenic solid state NMR: Challenges and solutions.Protein science : a publication of the Protein Society · 2024
    Review
  7. Review
  8. Contribution of protein conformational heterogeneity to NMR lineshapes at cryogenic temperatures.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  9. Article
  10. Resonant Mixing Dynamic Nuclear Polarization.The journal of physical chemistry letters · 2023
    Article
  11. Conformational ensembles explain NMR spectra of frozen intrinsically disordered proteins.Protein science : a publication of the Protein Society · 2023
    Article
  12. Article
  13. Article
  14. Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  15. Article
  16. Review
  17. Review
  18. Article
  19. Article
  20. Strategies for RNA Resonance Assignment byFrontiers in molecular biosciences · 2021
    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.

Ivan V SergeyevDepartment of Chemistry, Columbia University, New York, NY 10027.
Boris ItinNew York Structural Biology Center, New York, NY 10027.
Rivkah RogawskiDepartment of Chemistry, Columbia University, New York, NY 10027.
Loren A DayPublic Health Research Institute, Rutgers University, Newark, NJ 07103.
Ann E McDermottDepartment of Chemistry, Columbia University, New York, NY 10027; aem5@columbia.edu.ORCID 0000-0002-9249-1649

Funding

Structural and Functional Studies of Potassium Channels by Solid State NMRR01GM088724 · NIGMS · COLUMBIA UNIV NEW YORK MORNINGSIDE · PI ANN E MCDERMOTT · 2009 to 2026
$5.6M
TRAINING PROGRAM IN MOLECULAR BIOPHYSICST32GM008281 · NIGMS · COLUMBIA UNIV NEW YORK MORNINGSIDE · PI PALMER, ARTHUR G · 1988 to 2017
$5.4M
DYNAMIC NUCLEAR POLARIZATION SOLID STATE NMR SPECTROMETER FOR BIOMOLECULAR STUDIES10RR029249 · NCRR · NEW YORK STRUCTURAL BIOLOGY CENTER · PI MCDERMOTT, ANN E · 2010 to 2010
$2.3M
EXTRAMURAL RESEARCH FACILITIES CONSTRUCTIONC06RR015495 · NCRR · NEW YORK STRUCTURAL BIOLOGY CENTER · PI RIFKIND, RICHARD A · 2000 to 2000
$2.0M
NCRR NIH HHS C06 RR015495NCRR NIH HHS S10 RR029249NIGMS NIH HHS R01 GM088724NIGMS NIH HHS T32 GM008281
6 · The paper itself

Abstract

An experimental strategy has been developed to increase the efficiency of dynamic nuclear polarization (DNP) in solid-state NMR studies. The method makes assignments simpler, faster, and more reliable via sequential correlations of both side-chain and Cα resonances. The approach is particularly suited to complex biomolecules and systems with significant chemical-shift degeneracy. It was designed to overcome the spectral congestion and line broadening that occur due to sample freezing at the cryogenic temperatures required for DNP. Nonuniform sampling (NUS) is incorporated to achieve time-efficient collection of multidimensional data. Additionally, fast (25 kHz) magic-angle spinning (MAS) provides optimal sensitivity and resolution. Data collected in <1 wk produced a virtually complete de novo assignment of the coat protein of Pf1 virus. The peak positions and linewidths for samples near 100 K are perturbed relative to those near 273 K. These temperature-induced perturbations are strongly correlated with hydration surfaces.

Indexed as

Nuclear Magnetic Resonance, BiomolecularBacteriophage Pf1Pseudomonas aeruginosaDNPPf1 bacteriophageSSNMR

Identifiers

PMID28461483
PMCPMC5441803

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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.