Evidence map›Paper›PMID 18393447›Full record

ArticleBiochemistry2008

Monitoring aromatic picosecond to nanosecond dynamics in proteins via 13C relaxation: expanding perturbation mapping of the rigidifying core mutation, V54A, in eglin c.

Joshua A Boyer, Andrew L Lee

Abstract read
In one paragraph

Article in Biochemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

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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

23 citing papers in PubMed.

  1. Review
  2. Journal of biomolecular NMR · 2021
    Article
  3. Conformational exchange of aromatic side chains byJournal of biomolecular NMR · 2018
    Article
  4. Article
  5. Site-selectiveJournal of biomolecular NMR · 2017
    Article
  6. Site-selectiveJournal of biomolecular NMR · 2017
    Article
  7. Networks of Dynamic Allostery Regulate Enzyme Function.Structure (London, England : 1993) · 2017
    Article
  8. Bacterial production of site specificJournal of biomolecular NMR · 2017
    Article
  9. Article
  10. Prepaying the entropic cost for allosteric regulation in KIX.Proceedings of the National Academy of Sciences of the United States of America · 2014
    Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
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4 · The record

Corrections and comments

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5 · Who and what money

Authors and funding

2 authors.

Joshua A BoyerDepartment of Biochemistry and Biophysics, School of Medicine, University of North Carolina, Chapel Hill, North Carolina 27599, USA.
Andrew L Lee

Funding

Dynamic Networks and Mechanisms of Allosteric Communication in ProteinsR01GM066009 · NIGMS · UNIV OF NORTH CAROLINA CHAPEL HILL · PI LEE, ANDREW L · 2004 to 2012
$3.0M
NIGMS NIH HHS GM066009NIGMS NIH HHS R01 GM066009
6 · The paper itself

Abstract

Long-range effects, such as allostery, have evolved in proteins as a means of regulating function via communication between distal sites. An NMR-based perturbation mapping approach was used to more completely probe the dynamic response of the core mutation V54A in the protein eglin c by monitoring changes in picosecond to nanosecond aromatic side-chain dynamics and H/D exchange stabilities. Previous side-chain dynamics studies on this mutant were limited to methyl-bearing residues, most of which were found to rigidify on the picosecond to nanosecond time scale in the form of a contiguous "network". Here, high precision (13)C relaxation data from 13 aromatic side chains were acquired by applying canonical relaxation experiments to a newly developed carbon labeling scheme [Teilum et al. (2006) J. Am. Chem. Soc. 128, 2506-2507]. The fitting of model-free parameters yielded S (2) variability which is intermediate with respect to backbone and methyl-bearing side-chain variability and tau e values that are approximately 1 ns. Inclusion of the aromatic dynamic response results in an expanded network of dynamically coupled residues, with some aromatics showing increases in flexibility, which partially offsets the rigidification in methyl side chains. Using amide hydrogen exchange, dynamic propagation on a slower time scale was probed in response to the V54A perturbation. Surprisingly, regional stabilization (slowed exchange) 10-12 A from the site of mutation was observed despite a global destabilization of 1.5 kcal x mol (-1). Furthermore, this unlikely pocket of stabilized residues colocalizes with increases in aromatic flexibility on the faster time scale. Because the converse is also true (destabilized residues colocalize with rigidification on the fast time scale), a plausible entropy-driven mechanism is discussed for relating colocalization of opposing dynamic trends on vastly different time scales.

Indexed as

MovementMutationAmino Acids, AromaticCarbon IsotopesHydrogenKineticsMagnetic Resonance SpectroscopyModels, MolecularMutant ProteinsProtein ConformationProteinsThermodynamicsTime FactorsAmino Acids, AromaticCarbon Isotopeseglin proteinase inhibitorsHydrogenMutant ProteinsProteins

Identifiers

PMID18393447
PMCPMC3062916

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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.