ArticleCommunications chemistry2020
Quantifying the thermodynamics of protein unfolding using 2D NMR spectroscopy.
Article in Communications chemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
What it found
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Who cites it
11 citing papers in PubMed.
- Many Ways Out: Beyond the Two-State Model of Protein Unfolding.ACS omega · 2026Review
- Computational and Experimental Approaches and Applications of Biological NMR.Advances in experimental medicine and biology · 2026Review
- Prediction of mutation-induced protein stability changes based on the geometric representations learned by a self-supervised method.BMC bioinformatics · 2024Article
- Residue-based correlation between equilibrium and rate constants is an experimental formulation of the consistency principle for smooth structural changes of proteins.Biophysics and physicobiology · 2023Article
- Recipes for Inducing Cold Denaturation in an Otherwise Stable Protein.Journal of the American Chemical Society · 2022Article
- Heat and cold denaturation of yeast frataxin: The effect of pressure.Biophysical journal · 2022Article
- Protein Mutations and Stability, a Link with Disease: The Case Study of Frataxin.Biomedicines · 2022Review
- Temperature-Controlled Electrospray Ionization: Recent Progress and Applications.Chemistry (Weinheim an der Bergstrasse, Germany) · 2021Review
- The anatomy of unfolding of Yfh1 is revealed by site-specific fold stability analysis measured by 2D NMR spectroscopy.Communications chemistry · 2021Article
- Minimizing Pervasive Artifacts in 4D Covariance Maps for Protein Side Chain NMR Assignments.The journal of physical chemistry. A · 2021Article
- Thermal Analysis of a Mixture of Ribosomal Proteins by vT-ESI-MS: Toward a Parallel Approach for Characterizing theAnalytical chemistry · 2021Article
Corrections and comments
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Authors and funding
6 authors.
Funding
Abstract
A topic that has attracted considerable interest in recent years is the possibility to perform thermodynamic studies of proteins directly in-cell or in complex environments which mimic the cellular interior. Nuclear magnetic resonance (NMR) could be an attractive technique for these studies but its applicability has so far been limited by technical issues. Here, we demonstrate that 2D NMR methods can be successfully applied to measure thermodynamic parameters provided that a suitable choice of the residues used for the calculation is made. We propose a new parameter, named RAD, which reflects the level of protection of a specific amide proton in the protein core and can guide through the selection of the resonances. We also suggest a way to calibrate the volumes to become independent of technical limitations. The methodology we propose leads to stability curves comparable to that calculated from CD data and provides a new tool for thermodynamic measurements in complex environments.
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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.