ArticleACS omega2022
Exploring Structures and Dynamics of Protamine Molecules through Molecular Dynamics Simulations.
Article in ACS omega, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 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.
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.
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Who cites it
10 citing papers in PubMed, 17 citations in OpenAlex.
- Multivalent cations stabilize DNA duplexes beyond charge neutralization.Chemical science · 2026Article
- Investigation on the protective effects of the color stability of phycocyanin in vitro.Food chemistry: X · 2025Article
- Protamine Drives Liquid and Solid Condensation of DNA and Glycosaminoglycans.Langmuir : the ACS journal of surfaces and colloids · 2025Article
- Insights on the binding mechanisms and structural dynamics of protamine-DNA interaction.Biophysical reviews · 2025Review
- Polyethylene Glycolylation of the Purified Basic Protein (Protamine) of Squid (International journal of molecular sciences · 2025Article
- PROTA: A Robust Tool for Protamine Prediction Using a Hybrid Approach of Machine Learning and Deep Learning.International journal of molecular sciences · 2024Article
- Map conformational landscapes of intrinsically disordered proteins with polymer physics quantities.Biophysical journal · 2024Article
- Antimicrobial Peptide Recognition Motif of the Substrate Binding Protein SapA from NontypeableBiochemistry · 2024Article
- Reverse Engineering of a Pathogenic Antibody Reveals the Molecular Mechanism of Vaccine-Induced Immune Thrombotic Thrombocytopenia.Journal of the American Chemical Society · 2023Article
- Protamine folds DNA into flowers and loop stacks.Biophysical journal · 2023Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Protamines are arginine-rich proteins that condense DNA in sperm. Despite their importance in reproduction, information on protamine structure is scarce. We, therefore, used molecular dynamics to examine the structures of salmon, bull P1, and human P1 protamines. The sizes and shapes of each protamine varied widely, indicating that they were disordered with structures covering a broad conformational landscape, from hairpin loop structures to extended coils. Despite their general disorder, the protamines did form secondary structures, including helices and hairpin loops. In eutherians, hairpins may promote disulfide bonding that facilitates protamine-DNA condensation, but the specifics of this bonding is not well established. We examined inter-residue distances in the simulations to predict residue pairs likely to form intramolecular bonds, leading to the identification of bonding pairs consistent with previous results in bull and human. These results support a model for eutherian protamine structures where a highly charged center is surrounded by disulfide-bond-stabilized loops.
Identifiers
What OpenQuestion holds
Registered trials
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.