ArticleMethods in enzymology2018
Using NMR Chemical Shifts to Determine Residue-Specific Secondary Structure Populations for Intrinsically Disordered Proteins.
Article in Methods in enzymology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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15 citing papers in PubMed, 18 citations in OpenAlex.
- A Data Set of Simple 1-D and 2-D NMR Spectra of Peptides, including All Encoded Amino Acids, for Introductory Instruction in Protein Biomolecular NMR Spectroscopy.Biochemistry · 2026Article
- Characterization of flexible RNA binding by tandem RNA recognition motifs through integrative ensemble modelling.Nucleic acids research · 2026Article
- Plant-Based Protein Bioinks with Transglutaminase Crosslinking: 3D Printability and Molecular Insights from NMR and Synchrotron-FTIR.Foods (Basel, Switzerland) · 2026Article
- DR and SPIT: Statistical approaches for identifying transient structure in intrinsically disordered proteins via NMR chemical shifts.Protein science : a publication of the Protein Society · 2025Article
- Sensing Protein Structural Transitions with Microfluidic Modulation Infrared Spectroscopy.Biosensors · 2025Article
- CoVAMPnet: Comparative Markov State Analysis for Studying Effects of Drug Candidates on Disordered Biomolecules.JACS Au · 2024Article
- Disordered-to-ordered transitions in assembly factors allow the complex II catalytic subunit to switch binding partners.Nature communications · 2024Article
- Protein disorder and autoinhibition: The role of multivalency and effective concentration.Current opinion in structural biology · 2023Review
- Complex Conformational Space of the RNA Polymerase II C-Terminal Domain upon Phosphorylation.The journal of physical chemistry. B · 2023Article
- The influence of random-coil chemical shifts on the assessment of structural propensities in folded proteins and IDPs.RSC advances · 2023Review
- Semaphorin 3A-Glycosaminoglycans Interaction as Therapeutic Target for Axonal Regeneration.Pharmaceuticals (Basel, Switzerland) · 2021Article
- HACANCOi: a new HJournal of biomolecular NMR · 2020Article
- Dispersion from CJournal of biomolecular NMR · 2020Article
- Disorder for Dummies: Functional Mutagenesis of Transient Helical Segments in Disordered Proteins.Methods in molecular biology (Clifton, N.J.) · 2020Article
- p53 Phosphomimetics Preserve Transient Secondary Structure but Reduce Binding to Mdm2 and MdmX.Biomolecules · 2019Article
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2 authors at 1 institution in 1 country.
Funding
Abstract
Protein disorder is a pervasive phenomenon in biology and a natural consequence of polymer evolution that facilitates cell signaling by organizing sites for posttranslational modifications and protein-protein interactions into arrays of short linear motifs that can be rearranged by RNA splicing. Disordered proteins are missing the long-range nonpolar interactions that form tertiary structures, but they often contain regions with residual secondary structure that are stabilized by protein binding. NMR spectroscopy is uniquely suited to detect residual secondary structure in a disordered protein and it can provide atomic resolution data on the structure and dynamics of disordered protein interaction sites. Here we describe how backbone chemical shifts are used for assigning residual secondary structure in disordered proteins and discuss some of the tools available for estimating secondary structure populations with a focus on disordered proteins containing different levels of alpha helical secondary structure which are stabilized by protein binding.
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