ArticleChemphyschem : a European journal of chemical physics and physical chemistry2021
Using Cross-Correlated Spin Relaxation to Characterize Backbone Dihedral Angle Distributions of Flexible Protein Segments.
Article in Chemphyschem : a European journal of chemical physics and physical chemistry, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed.
- Accurate Protein Dynamic Conformational Ensembles: Combining AlphaFold, MD, and AmideInternational journal of molecular sciences · 2025Article
- Local structure propensities in disordered proteins from cross-correlated NMR spin relaxation.Journal of biomolecular NMR · 2025Article
- A complete set of cross-correlated relaxation experiments for determining the protein backbone dihedral angles.Journal of biomolecular NMR · 2025Article
- NMR-driven structure-based drug discovery by unveiling molecular interactions.Communications chemistry · 2025Review
- Reweighting methods for elucidation of conformation ensembles of proteins.Current opinion in structural biology · 2022Review
- Tandem domain structure determination based on a systematic enumeration of conformations.Scientific reports · 2021Article
- Using Cross-Correlated Spin Relaxation to Characterize Backbone Dihedral Angle Distributions of Flexible Protein Segments.Chemphyschem : a European journal of chemical physics and physical chemistry · 2021Article
- Detecting anisotropic segmental dynamics in disordered proteins by cross-correlated spin relaxation.Magnetic resonance (Gottingen, Germany) · 2021Article
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4 authors.
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Abstract
Crucial to the function of proteins is their existence as conformational ensembles sampling numerous and structurally diverse substates. Despite this widely accepted notion there is still a high demand for meaningful and reliable approaches to characterize protein ensembles in solution. As it is usually conducted in solution, NMR spectroscopy offers unique possibilities to address this challenge. Particularly, cross-correlated relaxation (CCR) effects have long been established to encode both protein structure and dynamics in a compelling manner. However, this wealth of information often limits their use in practice as structure and dynamics might prove difficult to disentangle. Using a modern Maximum Entropy (MaxEnt) reweighting approach to interpret CCR rates of Ubiquitin, we demonstrate that these uncertainties do not necessarily impair resolving CCR-encoded structural information. Instead, a suitable balance between complementary CCR experiments and prior information is found to be the most crucial factor in mapping backbone dihedral angle distributions. Experimental and systematic deviations such as oversimplified dynamics appear to be of minor importance. Using Ubiquitin as an example, we demonstrate that CCR rates are capable of characterizing rigid and flexible residues alike, indicating their unharnessed potential in studying disordered proteins.
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