ArticleBMC structural biology2011
Secondary structure of protamine in sperm nuclei: an infrared spectroscopy study.
Article in BMC structural biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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.
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.
Who cites it
14 citing papers in PubMed, 36 citations in OpenAlex.
- From chromosomal protein disorder to chromatin phase separation.Epigenetics & chromatin · 2026Review
- Phosphorylation of the protamine-like protein from baculovirus affects its DNA binding and virus propagation.Nucleic acids research · 2025Article
- Insights on the binding mechanisms and structural dynamics of protamine-DNA interaction.Biophysical reviews · 2025Review
- PROTA: A Robust Tool for Protamine Prediction Using a Hybrid Approach of Machine Learning and Deep Learning.International journal of molecular sciences · 2024Article
- Anhydrous proton conductor consisting of protamine-monododecyl phosphate composite with self-assembled structure.RSC advances · 2023Article
- The role of bacterial transport systems in the removal of host antimicrobial peptides in Gram-negative bacteria.FEMS microbiology reviews · 2022Review
- Drying and temperature induced conformational changes of nucleic acids and stallion sperm chromatin in trehalose preservation formulations.Scientific reports · 2021Article
- Developmental origins of transgenerational sperm histone retention following ancestral exposures.Developmental biology · 2020Article
- Protamines from liverwort are produced by post-translational cleavage and C-terminal di-aminopropanelation of several male germ-specific H1 histones.The Journal of biological chemistry · 2019Article
- Assay of 1-hydroxypyrene via aggregation-induced quenching of the fluorescence of protamine-modified gold nanoclusters and 9-hydroxyphenanthrene-based sensitization.Mikrochimica acta · 2019Article
- Protamine-stabilized gold nanoclusters as a fluorescent nanoprobe for lead(II) via Pb(II)-Au(I) interaction.Mikrochimica acta · 2018Article
- BaltDC: purification, characterization and infrared spectroscopy of an antiplatelet DC protein isolated fromThe journal of venomous animals and toxins including tropical diseases · 2017Article
- Expression and purification of the full murine NPM2 and study of its interaction with protamines and histones.Biochemistry and biophysics reports · 2016Article
- MicroRNA-122 influences the development of sperm abnormalities from human induced pluripotent stem cells by regulating TNP2 expression.Stem cells and development · 2013Article
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 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundProtamines are small basic proteins that condense the DNA in mature spermatozoa. Typical protamines are of simple composition and very arginine-rich, usually in the range of 60-80%. Arginine residues are distributed in a number of stretches separated by neutral amino acids. We have used Fourier transform infrared spectroscopy (FTIR) to gain access for the first time to the secondary structure of protamines in sperm nuclei. This technique is particularly well suited to the study of DNA-bound protamine in whole nuclei since it is not affected by turbidity.
resultsWe show that DNA -bound salmon (salmine) and squid protamines contain α-helix, β-turns and a proportion of other structures not stabilized by intramolecular hydrogen bonding. No β-sheet was observed. In salmine, the α-helix amounted to ~20%, while in squid protamine it reached ~40%. In contrast, the structure not stabilized by intermolecular hydrogen bonding was more abundant in salmine (~40%) than in squid protamine (~20%). Both protamines contained ~40% β-turns. The different helical potential of salmine and squid protamine was confirmed by structure predictions and CD in the presence of trifluoroethanol.
conclusionDNA-bound protamine in sperm nuclei contains large amounts of defined secondary structure stabilized by intramolecular hydrogen bonding. Both salmine and squid protamine contain similar amounts of β-turns, but differ in the proportions of α-helix and non-hydrogen bonded conformations. In spite of the large differences in the proportions of secondary structure motifs between salmon and squid protamines, they appear to be equally efficient in promoting tight hexagonal packing of the DNA molecules in sperm nuclei.
Indexed as
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.