ArticleJournal of biomolecular NMR2011
Measuring 1HN temperature coefficients in invisible protein states by relaxation dispersion NMR spectroscopy.
Article in Journal of biomolecular NMR, 2011. 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.
- NMR methods for investigating functionally relevant biomolecular dynamics.Magnetic resonance letters · 2025Review
- Non-uniform sampling of similar NMR spectra and its application to studies of the interaction between alpha-synuclein and liposomes.Journal of biomolecular NMR · 2023Article
- A fine balance of hydrophobic-electrostatic communication pathways in a pH-switching protein.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Temperature dependence of NMR chemical shifts: Tracking and statistical analysis.Protein science : a publication of the Protein Society · 2020Article
- UsingProtein science : a publication of the Protein Society · 2018Article
- Multistep mutational transformation of a protein fold through structural intermediates.Protein science : a publication of the Protein Society · 2018Article
- Mechanism of Protein Denaturation: Partial Unfolding of the P22 Coat Protein I-Domain by Urea Binding.Biophysical journal · 2015Article
- A role for indels in the evolution of Cro protein folds.Proteins · 2013Article
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5 authors.
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Abstract
A method based on the Carr-Purcell-Meiboom-Gill relaxation dispersion experiment is presented for measuring the temperature coefficients of amide proton chemical shifts of low populated 'invisible' protein states that exchange with a 'visible' ground state on the millisecond time-scale. The utility of the approach is demonstrated with an application to an I58D mutant of the Pfl6 Cro protein that undergoes exchange between the native, folded state and a cold denatured, unfolded conformational ensemble that is populated at a level of 6% at 2.5°C. A wide distribution of amide temperature coefficients is measured for the unfolded state. The distribution is centered about -5.6 ppb/K, consistent with an absence of intra-molecular hydrogen bonds, on average. However, the large range of values (standard deviation of 2.1 ppb/K) strongly supports the notion that the unfolded state of the protein is not a true random coil polypeptide chain.
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