Evidence map›Paper›PMID 18845162›Full record

ArticleJournal of molecular biology2008

Thermodynamics and folding pathway of tetraloop receptor-mediated RNA helical packing.

Kirk A Vander Meulen, Jared H Davis, Trenton R Foster, M Thomas Record, Samuel E Butcher

Open access · greenAbstract read
In one paragraph

Article in Journal of molecular biology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.5field-weighted citation impact, top 19% of its field
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

17 citing papers in PubMed, 30 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Dynamics of riboswitches: Molecular simulations.Biochimica et biophysica acta · 2014
    Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Entropic origin of Mg2+-facilitated RNA folding.Proceedings of the National Academy of Sciences of the United States of America · 2012
    Article
  12. Article
  13. Article
  14. Compact intermediates in RNA folding.Annual review of biophysics · 2010
    Review
  15. Review
  16. Article
  17. 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

5 authors at 1 institution in 1 country.

Kirk A Vander MeulenDepartment of Biochemistry, University of Wisconsin-Madison, 433 Babcock Dr., Madison, WI 53706, USA.
Jared H Davis
Trenton R Foster
M Thomas Record
Samuel E Butcher
University of Wisconsin–Madison · US

Funding

WATER DISTRIB:PHYSICAL PROPERT:PIZZA &LMPS MOZZARELLA CHEESES:EARLY STAGE MATURP41RR002301 · NCRR · UNIVERSITY OF WISCONSIN-MADISON · PI MARKLEY, JOHN LUTE · 1985 to 2011
$13.0M
THERMODYNAMICS &MECHANISMS OF PROTEIN/DNA INTERACTIONSR37GM023467 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI RECORD, M. THOMAS · 1997 to 2006
$2.9M
THERMODYNAMICS &MECHANISMS OF PROTEIN-DNA INTERACTIONSR01GM023467 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI RECORD, M. THOMAS · 1985 to 2011
$2.1M
NCRR NIH HHS P41 RR002301NIGMS NIH HHS GM23467NIGMS NIH HHS R01 GM023467NIGMS NIH HHS R37 GM023467
6 · The paper itself

Abstract

Little is known about the thermodynamic forces that drive the folding pathways of higher-order RNA structure. In this study, we employ calorimetric [isothermal titration calorimetry (ITC) and differential scanning calorimetry (DSC)] and spectroscopic (NMR and UV) methods to characterize the thermodynamics of the GAAA tetraloop-receptor interaction, utilizing a previously described bivalent construct. ITC studies indicate that the bivalent interaction is enthalpy driven and highly stable, with a binding constant (K(obs)) of 5.5x10(6) M(-1) and enthalpy (DeltaH(obs)(o)) of -33.8 kcal/mol at 45 degrees C in 20 mM KCl and 2 mM MgCl(2). Thus, we derive the DeltaH(obs)(o) for a single tetraloop-receptor interaction to be -16.9 kcal/mol at these conditions. UV absorbance data indicate that an increase in base stacking quality contributes to the enthalpy of complex formation. These highly favorable thermodynamics are consistent with the known critical role for the tetraloop-receptor motif in the folding of large RNAs. Additionally, a significant heat capacity change (DeltaC(p,obs)(o)) of -0.24 kcal mol(-1) K(-1) was determined by ITC. DSC and UV-monitored thermal denaturation experiments indicate that the bivalent tetraloop-receptor construct follows a minimally five-state unfolding pathway and suggest the observed DeltaC(p,obs)(o) for the interaction results from a temperature-dependent unbound receptor RNA structure.

Indexed as

CalorimetryCalorimetry, Differential ScanningFluorescence Resonance Energy TransferHot TemperatureKineticsMutationNucleic Acid ConformationNucleic Acid HeteroduplexesProtein ConformationProtein DenaturationProtein FoldingRNASpectrophotometry, UltravioletTemperatureThermodynamicsNucleic Acid HeteroduplexesRNA

Identifiers

PMID18845162
PMCPMC2678012
OpenAlexW2036613831

What OpenQuestion holds

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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.