Evidence map›Paper›PMID 17603075›Full record

ArticleJournal of molecular biology2007

Affinity and specificity of protein U1A-RNA complex formation based on an additive component free energy model.

Bethany L Kormos, Yulia Benitex, Anne M Baranger, David L Beveridge

Open access · greenAbstract read
In one paragraph

Article in Journal of molecular biology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.9field-weighted citation impact, top 16% 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

14 citing papers in PubMed, 41 citations in OpenAlex.

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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

4 authors at 2 institutions in 1 country.

Bethany L KormosChemistry Department and Molecular Biophysics Program, Wesleyan University, Middletown, CT 06459, USA. bkormos@wesleyan.edu
Yulia Benitex
Anne M Baranger
David L Beveridge
Wesleyan University · USUniversity of Illinois Urbana-Champaign · US

Funding

BIOORGANIC BASIS FOR RNA/PROTEIN STABILITYR01GM056857 · NIGMS · WESLEYAN UNIVERSITY · PI BARANGER, ANNE M · 1998 to 2006
$1.6M
Theoretical and MD Simulation Studies of U1A-RNA Binding and SpecificityR15GM076490 · NIGMS · WESLEYAN UNIVERSITY · PI BEVERIDGE, DAVID LEWIS · 2006 to 2006
$242k
Molecular Dynamics of Induced Fit in U1A-RNA ComplexesF32GM072345 · NIGMS · WESLEYAN UNIVERSITY · PI KORMOS, BETHANY L · 2004 to 2006
$134k
NIGMS NIH HHS F32 GM02345NIGMS NIH HHS F32 GM072345NIGMS NIH HHS GM-076490NIGMS NIH HHS GM-56857NIGMS NIH HHS R01 GM056857NIGMS NIH HHS R15 GM076490
6 · The paper itself

Abstract

An MM-GBSA computational protocol was used to investigate wild-type U1A-RNA and F56 U1A mutant experimental binding free energies. The trend in mutant binding free energies compared to wild-type is well-reproduced. Following application of a linear-response-like equation to scale the various energy components, the binding free energies agree quantitatively with observed experimental values. Conformational adaptation contributes to the binding free energy for both the protein and the RNA in these systems. Small differences in DeltaGs are the result of different and sometimes quite large relative contributions from various energetic components. Residual free energy decomposition indicates differences not only at the site of mutation, but throughout the entire protein. MM-GBSA and ab initio calculations performed on model systems suggest that stacking interactions may nearly, but not completely, account for observed differences in mutant binding affinities. This study indicates that there may be different underlying causes of ostensibly similar experimentally observed binding affinities of different mutants, and thus recommends caution in the interpretation of binding affinities and specificities purely by inspection.

Indexed as

Computer SimulationHumansKineticsModels, MolecularMolecular ConformationMutationProtein BindingProtein BiosynthesisProtein ConformationProtein Structure, TertiaryRibonucleoprotein, U1 Small NuclearRNARNA-Binding ProteinsSoftwareStatic ElectricityThermodynamicsRibonucleoprotein, U1 Small NuclearRNARNA-Binding ProteinsU1A protein

Identifiers

PMID17603075
PMCPMC2034351
OpenAlexW1983113769

What OpenQuestion holds

Textmetadata
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.