ArticleThe journal of physical chemistry. B2020
Curvature and Torsion of Protein Main Chain as Local Order Parameters of Protein Unfolding.
Article in The journal of physical chemistry. B, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed.
- Computational and Experimental Approaches and Applications of Biological NMR.Advances in experimental medicine and biology · 2026Review
- Structural Analysis of theBiomolecules · 2024Article
- Predicted and Experimental NMR Chemical Shifts at Variable Temperatures: The Effect of Protein Conformational Dynamics.The journal of physical chemistry letters · 2024Review
- Einstein Model of a Graph to Characterize Protein Folded/Unfolded States.Molecules (Basel, Switzerland) · 2023Article
- The anatomy of unfolding of Yfh1 is revealed by site-specific fold stability analysis measured by 2D NMR spectroscopy.Communications chemistry · 2021Article
- Missense Mutations Modify the Conformational Ensemble of theFrontiers in molecular biosciences · 2021Article
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Authors and funding
7 authors.
Funding
Abstract
Thermal protein unfolding resembles a global (two-state) phase transition. At the local scale, protein unfolding is, however, heterogeneous and probe dependent. Here, we consider local order parameters defined by the local curvature and torsion of the protein main chain. Because chemical shifts (CS's) measured by NMR spectroscopy are extremely sensitive to the local atomic environment, CS has served as a local probe of thermal unfolding of proteins by varying the position of the atomic isotope along the amino acid sequence. The variation of the CS of each C
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