Evidence map›Paper›PMID 27614060›Full record

ArticleBiochimica et biophysica acta2016

Directed assembly of defined oligomeric photosynthetic reaction centres through adaptation with programmable extra-membrane coiled-coil interfaces.

David J K Swainsbury, Robert L Harniman, Natalie D Di Bartolo, Juntai Liu, William F M Harper, Alexander S Corrie, Michael R Jones

Abstract read
In one paragraph

Article in Biochimica et biophysica acta, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. 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

7 authors.

David J K SwainsburySchool of Biochemistry, Medical Sciences Building, University of Bristol, University Walk, Bristol BS8 1TD, United Kingdom.
Robert L HarnimanSchool of Chemistry, University of Bristol, Cantock's Close, Bristol BS8 1TS, United Kingdom.
Natalie D Di BartoloSchool of Biochemistry, Medical Sciences Building, University of Bristol, University Walk, Bristol BS8 1TD, United Kingdom.
Juntai LiuSchool of Biochemistry, Medical Sciences Building, University of Bristol, University Walk, Bristol BS8 1TD, United Kingdom.
William F M HarperSchool of Biochemistry, Medical Sciences Building, University of Bristol, University Walk, Bristol BS8 1TD, United Kingdom.
Alexander S CorrieSchool of Biochemistry, Medical Sciences Building, University of Bristol, University Walk, Bristol BS8 1TD, United Kingdom.
Michael R JonesSchool of Biochemistry, Medical Sciences Building, University of Bristol, University Walk, Bristol BS8 1TD, United Kingdom. Electronic address: m.r.jones@bristol.ac.uk.

Funding

Biotechnology and Biological Sciences Research Council BB/I022570/1Biotechnology and Biological Sciences Research Council BB/L01386X/1
6 · The paper itself

Abstract

A challenge associated with the utilisation of bioenergetic proteins in new, synthetic energy transducing systems is achieving efficient and predictable self-assembly of individual components, both natural and man-made, into a functioning macromolecular system. Despite progress with water-soluble proteins, the challenge of programming self-assembly of integral membrane proteins into non-native macromolecular architectures remains largely unexplored. In this work it is shown that the assembly of dimers, trimers or tetramers of the naturally monomeric purple bacterial reaction centre can be directed by augmentation with an α-helical peptide that self-associates into extra-membrane coiled-coil bundle. Despite this induced oligomerisation the assembled reaction centres displayed normal spectroscopic properties, implying preserved structural and functional integrity. Mixing of two reaction centres modified with mutually complementary α-helical peptides enabled the assembly of heterodimers in vitro, pointing to a generic strategy for assembling hetero-oligomeric complexes from diverse modified or synthetic components

Indexed as

Energy MetabolismPhotosynthesisAdaptation, PhysiologicalBacterial ProteinsKineticsLightLight-Harvesting Protein ComplexesMolecular Dynamics SimulationPhotosynthetic Reaction Center Complex ProteinsProtein Conformation, alpha-HelicalProtein MultimerizationProteobacteriaStructure-Activity RelationshipBacterial ProteinsLight-Harvesting Protein ComplexesPhotosynthetic Reaction Center Complex ProteinsPufL protein, BacteriaPufM protein, BacteriaCoiled-coilDirected self-assemblyMembrane proteinOligomerisationPhotosystemReaction centre

Identifiers

PMID27614060
PMCPMC5084686

What OpenQuestion holds

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LicenceCC BY
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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.