Evidence map›Paper›PMID 26723586›Full record

ArticleThe Journal of chemical physics2015

Predictive energy landscapes for folding membrane protein assemblies.

Ha H Truong, Bobby L Kim, Nicholas P Schafer, Peter G Wolynes

Abstract read
In one paragraph

Article in The Journal of chemical physics, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
1.0field-weighted citation impact, top 30% 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

9 citing papers in PubMed, 15 citations in OpenAlex.

  1. Article
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  8. Review
  9. Topological constraints and modular structure in the folding and functional motions of GlpG, an intramembrane protease.Proceedings of the National Academy of Sciences of the United States of America · 2016
    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

4 authors at 2 institutions in 2 countries.

Ha H TruongDepartment of Chemistry, Rice University, Houston, Texas 77005, USA.
Bobby L KimDepartment of Chemistry, Rice University, Houston, Texas 77005, USA.
Nicholas P SchaferCenter for Theoretical Biological Physics, Rice University, Houston, Texas 77005, USA.
Peter G WolynesDepartment of Chemistry, Rice University, Houston, Texas 77005, USA.
Rice University · USCenter for Theoretical Biological Physics · US

Funding

CONCEPTUAL ASPECTS OF THE PROTEIN FOLDING PROBLEMR01GM044557 · NIGMS · UNIVERSITY OF ILLINOIS URBANA-CHAMPAIGN · PI WOLYNES, PETER GUY · 1990 to 2018
$4.2M
NIGMS NIH HHS R01 GM044557NIGMS NIH HHS R01 GM44557
6 · The paper itself

Abstract

We study the energy landscapes for membrane protein oligomerization using the Associative memory, Water mediated, Structure and Energy Model with an implicit membrane potential (AWSEM-membrane), a coarse-grained molecular dynamics model previously optimized under the assumption that the energy landscapes for folding α-helical membrane protein monomers are funneled once their native topology within the membrane is established. In this study we show that the AWSEM-membrane force field is able to sample near native binding interfaces of several oligomeric systems. By predicting candidate structures using simulated annealing, we further show that degeneracies in predicting structures of membrane protein monomers are generally resolved in the folding of the higher order assemblies as is the case in the assemblies of both nicotinic acetylcholine receptor and V-type Na(+)-ATPase dimers. The physics of the phenomenon resembles domain swapping, which is consistent with the landscape following the principle of minimal frustration. We revisit also the classic Khorana study of the reconstitution of bacteriorhodopsin from its fragments, which is the close analogue of the early Anfinsen experiment on globular proteins. Here, we show the retinal cofactor likely plays a major role in selecting the final functional assembly.

Indexed as

Molecular Dynamics SimulationProtein FoldingBacteriorhodopsinsBacteriorhodopsins

Identifiers

PMID26723586
PMCPMC4552702
OpenAlexW1180302593

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.