Evidence map›Paper›PMID 11566797›Full record

ArticleBiophysical journal2001

Simulated refolding of stretched titin immunoglobulin domains.

M Gao, H Lu, K Schulten

Abstract read
In one paragraph

Article in Biophysical journal, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing 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

20 citing papers in PubMed.

  1. Contribution of hydrophobic interactions to protein mechanical stability.Computational and structural biotechnology journal · 2022
    Article
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  10. Discovery through the computational microscope.Structure (London, England : 1993) · 2009
    Review
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  12. Article
  13. Review
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  20. Unfolding of titin domains studied by molecular dynamics simulations.Journal of muscle research and cell motility · 2002
    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

3 authors.

M GaoDepartment of Physics, University of Illinois at Urbana-Champaign, Urbana, Illinois 61801, USA.
H Lu
K Schulten

Funding

WHOLE CELL SIMULATIONP41RR005969 · NCRR · UNIVERSITY OF ILLINOIS URBANA-CHAMPAIGN · PI LUTHEY-SCHULTEN, ZAIDA · 1990 to 2011
$19.8M
NCRR NIH HHS 5 P41 RR05969
6 · The paper itself

Abstract

Steered molecular dynamics (SMD) is used to investigate forced unfolding and spontaneous refolding of immunoglobulin I27, a domain of the muscle protein titin. Previous SMD simulations revealed the events leading to stretch-induced unfolding of I27, the rupture of hydrogen bonds bridging beta-strands A and B, and those bridging beta-strands A' and G, the latter rupture occurring at an extension of approximately 15 A and preceding the complete unfolding. Simulations are now used to study the refolding of partially unfolded I27 domains. The results reveal that stretched domains with ruptured interstrand hydrogen bonds shrink along the extension direction. Two types of refolding patterns are recognized: for separated beta-strands A' and G, in most simulations five of the six hydrogen bonds between A' and G stably reformed in 2 ns, whereas for separated beta-strands A and B hydrogen bonds seldom reformed in eight 2-ns simulations. The mechanical stability of the partially refolded intermediates has been tested by re-stretching.

Indexed as

Models, MolecularProtein FoldingConnectinElasticityHydrogen BondingImmunoglobulinsMolecular MimicryMuscle ProteinsProtein KinasesProtein Structure, TertiarySolventsThermodynamicsWaterConnectinImmunoglobulinsMuscle ProteinsProtein KinasesSolventsWater

Identifiers

PMID11566797
PMCPMC1301698

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.