ArticleJournal of molecular biology2012
Protein structure determination from pseudocontact shifts using ROSETTA.
Article in Journal of molecular biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers.
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Who cites it
52 citing papers in PubMed.
- Bridging structure and function: artificial intelligence-based modelling of kidney proteins.Nature reviews. Nephrology · 2026Review
- Beyond structures: solution NMR as the quantitative engine of integrated structural biology.Frontiers in molecular biosciences · 2026Review
- Probing Biomolecular Interactions with Paramagnetic Nuclear Magnetic Resonance Spectroscopy.Chembiochem : a European journal of chemical biology · 2025Review
- Mononuclear binding and catalytic activity of europium(III) and gadolinium(III) at the active site of the model metalloenzyme phosphotriesterase.Acta crystallographica. Section D, Structural biology · 2024Article
- Structural Evolution of Paramagnetic Lanthanide Compounds in Solution Compared to Time- and Ensemble-Average Structures.Journal of the American Chemical Society · 2023Article
- Sparse pseudocontact shift NMR data obtained from a non-canonical amino acid-linked lanthanide tag improves integral membrane protein structure prediction.Journal of biomolecular NMR · 2023Article
- Recent Advances in NMR Protein Structure Prediction with ROSETTA.International journal of molecular sciences · 2023Review
- Modeling of protein conformational changes with Rosetta guided by limited experimental data.Structure (London, England : 1993) · 2022Article
- Incorporation of residual chemical shift anisotropy into the treatment ofJournal of magnetic resonance (San Diego, Calif. : 1997) · 2022Article
- Paramagnetic Chemical Probes for Studying Biological Macromolecules.Chemical reviews · 2022Review
- An engineered construct of cFLIP provides insight into DED1 structure and interactions.Structure (London, England : 1993) · 2022Article
- Characterizing conformational ensembles of multi-domain proteins using anisotropic paramagnetic NMR restraints.Biophysical reviews · 2022Review
- Localising nuclear spins by pseudocontact shifts from a single tagging site.Magnetic resonance (Gottingen, Germany) · 2022Article
- Paramagnetic Solid-State NMR to Localize the Metal-Ion Cofactor in an Oligomeric DnaB Helicase.Chemistry (Weinheim an der Bergstrasse, Germany) · 2021Article
- Methods for Molecular Modelling of Protein Complexes.Methods in molecular biology (Clifton, N.J.) · 2021Review
- Paramagnetic NMR in drug discovery.Journal of biomolecular NMR · 2020Review
- Macromolecular modeling and design in Rosetta: recent methods and frameworks.Nature methods · 2020Review
- A Practical Perspective on the Roles of Solution NMR Spectroscopy in Drug Discovery.Molecules (Basel, Switzerland) · 2020Review
- Insights into Structures and Dynamics of Flavivirus Proteases from NMR Studies.International journal of molecular sciences · 2020Review
- Paramagpy: software for fitting magnetic susceptibility tensors using paramagnetic effects measured in NMR spectra.Magnetic resonance (Gottingen, Germany) · 2020Article
Corrections and comments
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Authors and funding
5 authors.
Funding
Abstract
Paramagnetic metal ions generate pseudocontact shifts (PCSs) in nuclear magnetic resonance spectra that are manifested as easily measurable changes in chemical shifts. Metals can be incorporated into proteins through metal binding tags, and PCS data constitute powerful long-range restraints on the positions of nuclear spins relative to the coordinate system of the magnetic susceptibility anisotropy tensor (Δχ-tensor) of the metal ion. We show that three-dimensional structures of proteins can reliably be determined using PCS data from a single metal binding site combined with backbone chemical shifts. The program PCS-ROSETTA automatically determines the Δχ-tensor and metal position from the PCS data during the structure calculations, without any prior knowledge of the protein structure. The program can determine structures accurately for proteins of up to 150 residues, offering a powerful new approach to protein structure determination that relies exclusively on readily measurable backbone chemical shifts and easily discriminates between correctly and incorrectly folded conformations.
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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.