Evidence map›Paper›PMID 18844399›Full record

ArticleThe journal of physical chemistry. B2008

Furanose dynamics in the HhaI methyltransferase target DNA studied by solution and solid-state NMR relaxation.

Dorothy Echodu, Gil Goobes, Zahra Shajani, Kari Pederson, Gary Meints, Gabriele Varani, Gary Drobny

Abstract read
In one paragraph

Article in The journal of physical chemistry. B, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing 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

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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

15 citing papers in PubMed.

  1. Article
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  3. Article
  4. Article
  5. Article
  6. Article
  7. Protein dynamics in the solid-state fromSolid state nuclear magnetic resonance · 2018
    Article
  8. Article
  9. Article
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  12. Article
  13. Review
  14. Article
  15. 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

7 authors.

Dorothy EchoduDepartment of Chemistry, University of Washington, Seattle, WA 98195-1700, USA.
Gil Goobes
Zahra Shajani
Kari Pederson
Gary Meints
Gabriele Varani
Gary Drobny

Funding

Dynamic Aspects of Nucleic Acid-Protein RecognitionR01EB003152 · NIBIB · UNIVERSITY OF WASHINGTON · PI DROBNY, GARY PETER · 2004 to 2011
$3.3M
NIBIB NIH HHS R01 EB003152NIBIB NIH HHS R01 EB03152
6 · The paper itself

Abstract

Both solid-state and solution NMR relaxation measurements are routinely used to quantify the internal dynamics of biomolecules, but in very few cases have these two techniques been applied to the same system, and even fewer attempts have been made so far to describe the results obtained through these two methods through a common theoretical framework. We have previously collected both solution 13C and solid-state 2H relaxation measurements for multiple nuclei within the furanose rings of several nucleotides of the DNA sequence recognized by HhaI methyltransferase. The data demonstrated that the furanose rings within the GCGC recognition sequence are very flexible, with the furanose rings of the cytidine, which is the methylation target, experiencing the most extensive motions. To interpret these experimental results quantitatively, we have developed a dynamic model of furanose rings based on the analysis of solid-state 2H line shapes. The motions are modeled by treating bond reorientations as Brownian excursions within a restoring potential. By applying this model, we are able to reproduce the rates of 2H spin-lattice relaxation in the solid and 13C spin-lattice relaxation in solution using comparable restoring force constants and internal diffusion coefficients. As expected, the 13C relaxation rates in solution are less sensitive to motions that are slower than overall molecular tumbling than to the details of global molecular reorientation, but are somewhat more sensitive to motions in the immediate region of the Larmor frequency. Thus, we conclude that the local internal motions of this DNA oligomer in solution and in the hydrated solid state are virtually the same, and we validate an approach to the conjoint analysis of solution and solid-state NMR relaxation and line shapes data, with wide applicability to many biophysical problems.

Indexed as

CarbohydratesComputer SimulationDeuteriumDNADNA-Cytosine MethylasesModels, MolecularNuclear Magnetic Resonance, BiomolecularNucleic Acid ConformationTime FactorsCarbohydratesDeuteriumDNADNA-Cytosine MethylasesDNA modification methylase HhaI

Identifiers

PMID18844399
PMCPMC2735271

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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.