ArticleJournal of biomolecular NMR2012
Identification of helix capping and b-turn motifs from NMR chemical shifts.
Article in Journal of biomolecular NMR, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.
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Who cites it
47 citing papers in PubMed, 91 citations in OpenAlex.
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- The structure of Vibrio cholerae FeoC reveals conservation of the helix-turn-helix motif but not the cluster-binding domain.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2022Article
- Combined High-Pressure and Multiquantum NMR and Molecular Simulation Propose a Role for N-Terminal Salt Bridges in Amyloid-Beta.The journal of physical chemistry letters · 2021Article
- Structural basis of PETISCO complex assembly during piRNA biogenesis inGenes & development · 2021Article
- Structural Analysis of the Menangle Virus P Protein Reveals a Soft Boundary between Ordered and Disordered Regions.Viruses · 2021Article
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- Order and disorder-An integrative structure of the full-length human growth hormone receptor.Science advances · 2021Article
- Discovery of a Highly Conserved Peptide in the Iron Transporter Melanotransferrin that Traverses an Intact Blood Brain Barrier and Localizes in Neural Cells.Frontiers in neuroscience · 2021Article
- Hybrid methods for combined experimental and computational determination of protein structure.The Journal of chemical physics · 2020Review
- Structural, Dynamic, and Functional Characterization of a DnaX Mini-intein Derived fromBiochemistry · 2020Article
- Structural Insights into N-terminal IgV Domain of BTNL2, a T Cell Inhibitory Molecule, Suggests a Non-canonical Binding Interface for Its Putative Receptors.Journal of molecular biology · 2020Article
- Deciphering the activation and recognition mechanisms of Staphylococcus aureus response regulator ArlR.Nucleic acids research · 2019Article
- Disordered region of H3K9 methyltransferase Clr4 binds the nucleosome and contributes to its activity.Nucleic acids research · 2019Article
- The Effects of One Amino Acid Substitutions at the C-Terminal Region of Thermostable L2 Lipase by Computational and Experimental Approach.Molecular biotechnology · 2018Article
- Tsg101 chaperone function revealed by HIV-1 assembly inhibitors.Nature communications · 2017Article
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2 authors at 1 institution in 1 country.
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Abstract
We present an empirical method for identification of distinct structural motifs in proteins on the basis of experimentally determined backbone and (13)C(β) chemical shifts. Elements identified include the N-terminal and C-terminal helix capping motifs and five types of β-turns: I, II, I', II' and VIII. Using a database of proteins of known structure, the NMR chemical shifts, together with the PDB-extracted amino acid preference of the helix capping and β-turn motifs are used as input data for training an artificial neural network algorithm, which outputs the statistical probability of finding each motif at any given position in the protein. The trained neural networks, contained in the MICS (motif identification from chemical shifts) program, also provide a confidence level for each of their predictions, and values ranging from ca 0.7-0.9 for the Matthews correlation coefficient of its predictions far exceed those attainable by sequence analysis. MICS is anticipated to be useful both in the conventional NMR structure determination process and for enhancing on-going efforts to determine protein structures solely on the basis of chemical shift information, where it can aid in identifying protein database fragments suitable for use in building such structures.
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