Evidence map›Paper›PMID 19235934›Full record

ArticleJournal of the American Chemical Society2009

Correlated dynamics between protein HN and HC bonds observed by NMR cross relaxation.

Beat Vögeli, Lishan Yao

Abstract read
In one paragraph

Article in Journal of the American Chemical Society, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing 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

13 citing papers in PubMed.

  1. Article
  2. Article
  3. Distance-independent Cross-correlated Relaxation and Isotropic Chemical Shift Modulation in Protein Dynamics Studies.Chemphyschem : a European journal of chemical physics and physical chemistry · 2019
    Review
  4. Journal of biomolecular NMR · 2018
    Article
  5. Correlated motions of C'-N and CJournal of biomolecular NMR · 2018
    Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. 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

2 authors.

Beat VögeliLaboratory of Physical Chemistry, Swiss Federal Institute of Technology, ETH-Honggerberg, CH-8093 Zurich, Switzerland. beat.voegeli@phys.chem.ethz.ch
Lishan Yao

Funding

Protein structure and dynamics from residual dipolar couplingsZIADK029048 · NIDDK · NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES · PI BAX, ADRIAAN · 2009 to 2018
$4.6M
Protein structure and dynamics from residual dipolar couplingsZ01DK029048 · NIDDK · NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES · PI BAX, AD - · 2007 to 2008
$942k
Intramural NIH HHS NIH0012716609Intramural NIH HHS Z01 DK029048
6 · The paper itself

Abstract

Although collective dynamics of atom groups steer many biologically relevant processes in biomacromolecules, most atomic resolution motional studies focus on isolated bonds. In this study, a new method is introduced to assess correlated dynamics between bond vectors by cross relaxation nuclear magnetic resonance (NMR). Dipole-dipole cross correlated relaxation rates between intra- and inter-residual H(N)-N and H(alpha)-C(alpha) in the 56 residue protein GB3 are measured with high accuracy. It is demonstrated that the assumption of anisotropic molecular tumbling is necessary to evaluate rates accurately and predictions from the static structure using effective bond lengths of 1.041 and 1.117 A for H(N)-N and H(alpha)-C(alpha) are within 3% of both experimental intra- and inter-residual rates. Deviations are matched to models of different degrees of motional correlation. These models are based on previously determined orientations and motional amplitudes from residual dipolar couplings with high accuracy and precision. Clear evidence of correlated motion in the loops comprising residues 10-14, 20-22, and 47-50 and anticorrelated motion in the alpha helix comprising 23-38 is presented. Somewhat weaker correlation is observed in the beta strands 2-4, which have previously been shown to exhibit slow correlated motional modes.

Indexed as

Nuclear Magnetic Resonance, BiomolecularProteinsProteins

Identifiers

PMID19235934
PMCPMC2750032

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.