Evidence map›Paper›PMID 24613485›Full record

ArticleStructure (London, England : 1993)2014

Conformational analysis of processivity clamps in solution demonstrates that tertiary structure does not correlate with protein dynamics.

Jing Fang, Philip Nevin, Visvaldas Kairys, Česlovas Venclovas, John R Engen, Penny J Beuning

Abstract read
In one paragraph

Article in Structure (London, England : 1993), 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing 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

22 citing papers in PubMed.

  1. Article
  2. Article
  3. Review
  4. Beyond the mono-nucleosome.Biochemical Society transactions · 2025
    Review
  5. Review
  6. Article
  7. Differences in clamp loader mechanism between bacteria and eukaryotes.bioRxiv : the preprint server for biology · 2023
    Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. Review
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

6 authors.

Jing Fang *Department of Chemistry and Chemical Biology, Northeastern University, Boston, MA 02115, USA.
Philip Nevin *Department of Chemistry and Chemical Biology, Northeastern University, Boston, MA 02115, USA.
Visvaldas KairysInstitute of Biotechnology, Vilnius University, LT-02241 Vilnius, Lithuania.
Česlovas VenclovasInstitute of Biotechnology, Vilnius University, LT-02241 Vilnius, Lithuania.
John R EngenDepartment of Chemistry and Chemical Biology, Northeastern University, Boston, MA 02115, USA.
Penny J BeuningDepartment of Chemistry and Chemical Biology, Northeastern University, Boston, MA 02115, USA.

Funding

Protein conformational change upon membrane associationR01GM086507 · NIGMS · NORTHEASTERN UNIVERSITY · PI ENGEN, JOHN R · 2009 to 2012
$1.6M
Extending the applications of hydrogen exchange mass spectrometryR01GM101135 · NIGMS · NORTHEASTERN UNIVERSITY · PI ENGEN, JOHN R · 2012 to 2015
$1.2M
NIGMS NIH HHS R01 GM086507NIGMS NIH HHS R01-GM086507NIGMS NIH HHS R01 GM101135NIGMS NIH HHS R01-GM101135
6 · The paper itself

Abstract

The relationship between protein sequence, structure, and dynamics has been elusive. Here, we report a comprehensive analysis using an in-solution experimental approach to study how the conservation of tertiary structure correlates with protein dynamics. Hydrogen exchange measurements of eight processivity clamp proteins from different species revealed that, despite highly similar three-dimensional structures, clamp proteins display a wide range of dynamic behavior. Differences were apparent both for structurally similar domains within proteins and for corresponding domains of different proteins. Several of the clamps contained regions that underwent local unfolding with different half-lives. We also observed a conserved pattern of alternating dynamics of the α helices lining the inner pore of the clamps as well as a correlation between dynamics and the number of salt bridges in these α helices. Our observations reveal that tertiary structure and dynamics are not directly correlated and that primary structure plays an important role in dynamics.

Indexed as

Molecular Dynamics SimulationArabidopsisBacteriophage T4DNA Polymerase IIIEscherichia coliGene ExpressionHalf-LifeHumansProtein BindingProtein FoldingProtein MultimerizationProtein Structure, SecondaryProtein Structure, TertiaryRecombinant ProteinsSaccharomyces cerevisiaeSpecies SpecificityDNA Polymerase IIIRecombinant Proteins

Identifiers

PMID24613485
PMCPMC3984358

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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.