ArticleBiophysical journal2005
The influence of protein-protein interactions on the organization of proteins within thylakoid membranes.
Article in Biophysical journal, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
What it found
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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.
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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.
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Who cites it
7 citing papers in PubMed, 19 citations in OpenAlex.
- Unraveling design principles of protein landscapes in photosynthetic membranes in plant chloroplasts.Science advances · 2026Article
- Biological physics by high-speed atomic force microscopy.Philosophical transactions. Series A, Mathematical, physical, and engineering sciences · 2020Review
- Molecular dynamics simulations in photosynthesis.Photosynthesis research · 2020Review
- Coexistence of fluid and crystalline phases of proteins in photosynthetic membranes.Biophysical journal · 2013Article
- Coarse-grained computer simulation of dynamics in thylakoid membranes: methods and opportunities.Frontiers in plant science · 2013Review
- Differential mobility of pigment-protein complexes in granal and agranal thylakoid membranes of C₃ and C₄ plants.Plant physiology · 2013Article
- Organization of membrane-associated proteins in lipid bilayers.The European physical journal. E, Soft matter · 2008Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The influence of attractive protein-protein interactions on the organization of photosynthetic proteins within the thylakoid membrane was investigated. Protein-protein interactions were simulated using Monte Carlo techniques and the influence of different interaction energies was examined. It was found that weak interactions led to protein clusters whereas strong interactions led to ramified chains. An optimum curve for the relationship between interaction energy and the number of contact sites emerged. With increasing particle densities the effect decreased. In a mixture of interacting and noninteracting particles the distance between the noninteracting particles was increased and there seemed to be much more free space around them. In thylakoids, this could lead to a more homogeneous distribution of the noninteracting but rate-limiting cytochrome bf complexes. Due to the increased free space between cytochrome bf, obstruction of binding sites--occurring unavoidably in a random distribution--may be drastically reduced. Furthermore, protein-protein interactions in thylakoids may lead to a decrease in plastoquinone diffusion.
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Registered trials
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