ArticleNature communications2019
Methionine in a protein hydrophobic core drives tight interactions required for assembly of spider silk.
Article in Nature communications, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 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
19 citing papers in PubMed, 39 citations in OpenAlex.
- Dynamics-aware evolutionary profiling uncouples structural rigidity from functional motion to enable enhanced variant interpretation.Functional & integrative genomics · 2026Article
- Ultratight Binding of a Capture Spiral Spider Silk Protein through Electrostatic Forces.ACS bio & med chem Au · 2026Article
- Emergent properties of supramolecular peptide assemblies.Chemical communications (Cambridge, England) · 2026Review
- Laccases from lactic acid bacteria show cuprous oxidase activity and capture Cu(II) and Ag(I) ions.Protein science : a publication of the Protein Society · 2026Article
- A newly evolved small secretory peptide enhances mechanical properties of spider silk.Nature communications · 2025Article
- Article
- Combined clinical, structural and cellular studies discriminate pathogenic and benign TRPV4 variants.Brain : a journal of neurology · 2025Article
- Domain swap facilitates structural transitions of spider silk protein C-terminal domains.Protein science : a publication of the Protein Society · 2023Article
- Variation among arthropod taxa in the amino acid content of exoskeleton and digestible tissue.Ecology and evolution · 2023Article
- Unusual pBiomacromolecules · 2023Article
- Chemoselective Methionine Labelling of Recombinant Trastuzumab Shows High In Vitro and In Vivo Tumour Targeting.Chemistry (Weinheim an der Bergstrasse, Germany) · 2023Article
- Increasing the OACS catalysis · 2023Article
- Spidroin N-terminal domain forms amyloid-like fibril based hydrogels and provides a protein immobilization platform.Nature communications · 2022Article
- The dimerization mechanism of the N-terminal domain of spider silk proteins is conserved despite extensive sequence divergence.The Journal of biological chemistry · 2022Article
- Customized Flagelliform Spidroins Form Spider Silk-like Fibers at pH 8.0 with Outstanding Tensile Strength.ACS biomaterials science & engineering · 2022Article
- Solution Structure of Tubuliform Spidroin N-Terminal Domain and Implications for pH Dependent Dimerization.Frontiers in molecular biosciences · 2022Article
- Effect of Met/Leu substitutions on the stability of NAD+-dependent formate dehydrogenases from Gossypium hirsutum.Applied microbiology and biotechnology · 2021Article
- High intracellular stability of the spidroin N-terminal domain in spite of abundant amyloidogenic segments revealed by in-cell hydrogen/deuterium exchange mass spectrometry.The FEBS journal · 2020Article
- Structure, interdomain dynamics, and pH-dependent autoactivation of pro-rhodesain, the main lysosomal cysteine protease from African trypanosomes.The Journal of biological chemistryArticle
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 3 institutions in 2 countries.
Funding
Abstract
Web spiders connect silk proteins, so-called spidroins, into fibers of extraordinary toughness. The spidroin N-terminal domain (NTD) plays a pivotal role in this process: it polymerizes spidroins through a complex mechanism of dimerization. Here we analyze sequences of spidroin NTDs and find an unusually high content of the amino acid methionine. We simultaneously mutate all methionines present in the hydrophobic core of a spidroin NTD from a nursery web spider's dragline silk to leucine. The mutated NTD is strongly stabilized and folds at the theoretical speed limit. The structure of the mutant is preserved, yet its ability to dimerize is substantially impaired. We find that side chains of core methionines serve to mobilize the fold, which can thereby access various conformations and adapt the association interface for tight binding. Methionine in a hydrophobic core equips a protein with the capacity to dynamically change shape and thus to optimize its function.
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.