Evidence map›Paper›PMID 24912167›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2014

Accounting for a mirror-image conformation as a subtle effect in protein folding.

Khatuna Kachlishvili, Gia G Maisuradze, Osvaldo A Martin, Adam Liwo, Jorge A Vila, Harold A Scheraga

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing 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

12 citing papers in PubMed.

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  11. My 65 years in protein chemistry.Quarterly reviews of biophysics · 2015
    Review
  12. Review
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

6 authors.

Khatuna KachlishviliBaker Laboratory of Chemistry and Chemical Biology, Cornell University, Ithaca, NY 14853-1301;
Gia G MaisuradzeBaker Laboratory of Chemistry and Chemical Biology, Cornell University, Ithaca, NY 14853-1301;
Osvaldo A MartinBaker Laboratory of Chemistry and Chemical Biology, Cornell University, Ithaca, NY 14853-1301;Instituto de Matemática Aplicada San Luis, Consejo Nacional de Investigaciones Científicas y Técnicas de Argentina, Universidad Nacional de San Luis, 5700 San Luis, Argentina; and.
Adam LiwoLaboratory of Molecular Modeling, Faculty of Chemistry, University of Gdańsk, 80-308 Gdańsk, Poland.
Jorge A VilaBaker Laboratory of Chemistry and Chemical Biology, Cornell University, Ithaca, NY 14853-1301;Instituto de Matemática Aplicada San Luis, Consejo Nacional de Investigaciones Científicas y Técnicas de Argentina, Universidad Nacional de San Luis, 5700 San Luis, Argentina; and.
Harold A ScheragaBaker Laboratory of Chemistry and Chemical Biology, Cornell University, Ithaca, NY 14853-1301; has5@cornell.edu.

Funding

INTERNAL BONDIN IN PROTEINSR01GM014312 · NIGMS · CORNELL UNIVERSITY ITHACA · PI MAISURADZE, GIA, RACKOVSKY, SHALOM R · 1985 to 2021
$9.4M
NIGMS NIH HHS R01 GM014312
6 · The paper itself

Abstract

By using local (free-energy profiles along the amino acid sequence and (13)C(α) chemical shifts) and global (principal component) analyses to examine the molecular dynamics of protein-folding trajectories, generated with the coarse-grained united-residue force field, for the B domain of staphylococcal protein A, we are able to (i) provide the main reason for formation of the mirror-image conformation of this protein, namely, a slow formation of the second loop and part of the third helix (Asp29-Asn35), caused by the presence of multiple local conformational states in this portion of the protein; (ii) show that formation of the mirror-image topology is a subtle effect resulting from local interactions; (iii) provide a mechanism for how protein A overcomes the barrier between the metastable mirror-image state and the native state; and (iv) offer a plausible reason to explain why protein A does not remain in the metastable mirror-image state even though the mirror-image and native conformations are at least energetically compatible.

Indexed as

Protein ConformationProtein FoldingProtein Structure, SecondaryAlgorithmsAmino Acid SequenceKineticsModels, ChemicalModels, MolecularMolecular Dynamics SimulationMolecular Sequence DataPrincipal Component AnalysisProteinsStaphylococcal Protein AThermodynamicsTime FactorsProteinsStaphylococcal Protein Amisfoldingsymmetrical proteins

Identifiers

PMID24912167
PMCPMC4060689

What OpenQuestion holds

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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.