Evidence map›Paper›PMID 20159163›Full record

ArticleBiophysical journal2010

Thermo- and mesostabilizing protein interactions identified by temperature-dependent statistical potentials.

Benjamin Folch, Yves Dehouck, Marianne Rooman

Abstract read
In one paragraph

Article in Biophysical journal, 2010. 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

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

23 citing papers in PubMed.

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  9. Bispecific antibodies-effects of point mutations on CH3-CH3 interface stability.Protein engineering, design & selection : PEDS · 2022
    Article
  10. Article
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  17. Improved insights into protein thermal stability: from the molecular to the structurome scale.Philosophical transactions. Series A, Mathematical, physical, and engineering sciences · 2016
    Article
  18. Article
  19. Article
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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

3 authors.

Benjamin FolchUnité de Bioinformatique Génomique et Structurale, Université Libre de Bruxelles, Brussels, Belgium. bfolch@ulb.ac.be
Yves Dehouck
Marianne Rooman

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The goal of controlling protein thermostability is tackled here through establishing, by in silico analyses, the relative weight of residue-residue interactions in proteins as a function of temperature. We have designed for that purpose a (melting-) temperature-dependent, statistical distance potential, where the interresidue distances are computed between the side-chain geometric centers or their functional centers. Their separate derivation from proteins of either high or low thermal resistance reveals the interactions that contribute most to stability in different temperature ranges. Thermostabilizing interactions include salt bridges and cation-pi interactions (especially those involving arginine), aromatic interactions, and H-bonds between negatively charged and some aromatic residues. In contrast, H-bonds between two polar noncharged residues or between a polar noncharged residue and a negatively charged residue are relatively less stabilizing at high temperatures. An important observation is that it is necessary to consider both repulsive and attractive interactions in overall thermostabilization, as the degree of repulsion may also vary with temperature. These temperature-dependent potentials are not only useful for the identification of meso- and thermostabilizing pair interactions, but also exhibit predictive power, as illustrated by their ability to predict the melting temperature of a protein based on the melting temperature of homologous proteins.

Indexed as

Computational BiologyTemperatureAmino AcidsHydrogen BondingHydrophobic and Hydrophilic InteractionsProtein BindingProteinsProtein StabilitySequence Homology, Amino AcidTransition TemperatureAmino AcidsProteins

Identifiers

PMID20159163
PMCPMC2820637

What OpenQuestion holds

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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.