ArticleJournal of biomolecular NMR2008
Automated sequence-specific protein NMR assignment using the memetic algorithm MATCH.
Article in Journal of biomolecular NMR, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 55 papers.
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Who cites it
55 citing papers in PubMed.
- Modernizing biomolecular NMR: The POKY suite.The Journal of biological chemistry · 2026Review
- 5D solid-state NMR spectroscopy for facilitated resonance assignment.Journal of biomolecular NMR · 2023Article
- NMR Assignment through Linear Programming.Journal of global optimization : an international journal dealing with theoretical and computational aspects of seeking global optima and their applications in science, management and engineering · 2022Article
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- A ligand-induced structural change in fatty acid-binding protein 1 is associated with potentiation of peroxisome proliferator-activated receptor α agonists.The Journal of biological chemistry · 2019Article
- Automated projection spectroscopy in solid-state NMR.Journal of biomolecular NMR · 2018Review
- Molecular interactions connecting the function of the serine-arginine-rich protein SRSF1 to protein phosphatase 1.The Journal of biological chemistry · 2018Article
- Modern Technologies of Solution Nuclear Magnetic Resonance Spectroscopy for Three-dimensional Structure Determination of Proteins Open Avenues for Life Scientists.Computational and structural biotechnology journal · 2017Review
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- Fragment library screening identifies hits that bind to the non-catalytic surface of Pseudomonas aeruginosa DsbA1.PloS one · 2017Article
- NMR in structural genomics to increase structural coverage of the protein universe: Delivered by Prof. Kurt Wüthrich on 7 July 2013 at the 38th FEBS Congress in St. Petersburg, Russia.The FEBS journal · 2016Article
- Network representation of protein interactions: Theory of graph description and analysis.Protein science : a publication of the Protein Society · 2016Article
- Structure of fully protonated proteins by proton-detected magic-angle spinning NMR.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Dynamic Local Polymorphisms in the Gbx1 Homeodomain Induced by DNA Binding.Structure (London, England : 1993) · 2016Article
- The acidic domain is a unique structural feature of the splicing factor SYNCRIP.Protein science : a publication of the Protein Society · 2016Article
- Directional Phosphorylation and Nuclear Transport of the Splicing Factor SRSF1 Is Regulated by an RNA Recognition Motif.Journal of molecular biology · 2016Article
- UHM-ULM interactions in the RBM39-U2AF65 splicing-factor complex.Acta crystallographica. Section D, Structural biology · 2016Article
- Nuclear Magnetic Resonance Structure of a Novel Globular Domain in RBM10 Containing OCRE, the Octamer Repeat Sequence Motif.Structure (London, England : 1993) · 2016Article
- Structure and Mechanism of the Influenza A M218-60 Dimer of Dimers.Journal of the American Chemical Society · 2015Article
- Cofactor-induced reversible folding of Flavodoxin-4 from Lactobacillus acidophilus.Protein science : a publication of the Protein Society · 2015Article
Corrections and comments
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
MATCH (Memetic Algorithm and Combinatorial Optimization Heuristics) is a new memetic algorithm for automated sequence-specific polypeptide backbone NMR assignment of proteins. MATCH employs local optimization for tracing partial sequence-specific assignments within a global, population-based search environment, where the simultaneous application of local and global optimization heuristics guarantees high efficiency and robustness. MATCH thus makes combined use of the two predominant concepts in use for automated NMR assignment of proteins. Dynamic transition and inherent mutation are new techniques that enable automatic adaptation to variable quality of the experimental input data. The concept of dynamic transition is incorporated in all major building blocks of the algorithm, where it enables switching between local and global optimization heuristics at any time during the assignment process. Inherent mutation restricts the intrinsically required randomness of the evolutionary algorithm to those regions of the conformation space that are compatible with the experimental input data. Using intact and artificially deteriorated APSY-NMR input data of proteins, MATCH performed sequence-specific resonance assignment with high efficiency and robustness.
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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.