ArticleProtein science : a publication of the Protein Society2020
Temperature dependence of NMR chemical shifts: Tracking and statistical analysis.
Article in Protein science : a publication of the Protein Society, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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18 citing papers in PubMed, 34 citations in OpenAlex.
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- Evidence that the TRPV1 S1-S4 membrane domain contributes to thermosensing.Nature communications · 2020Article
- Temperature dependence of NMR chemical shifts: Tracking and statistical analysis.Protein science : a publication of the Protein Society · 2020Article
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4 authors at 1 institution in 1 country.
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Abstract
Isotropic chemical shifts measured by solution nuclear magnetic resonance (NMR) spectroscopy offer extensive insights into protein structure and dynamics. Temperature dependences add a valuable dimension; notably, the temperature dependences of amide proton chemical shifts are valuable probes of hydrogen bonding, temperature-dependent loss of structure, and exchange between distinct protein conformations. Accordingly, their uses include structural analysis of both folded and disordered proteins, and determination of the effects of mutations, binding, or solution conditions on protein energetics. Fundamentally, these temperature dependences result from changes in the local magnetic environments of nuclei, but correlations with global thermodynamic parameters measured via calorimetric methods have been observed. Although the temperature dependences of amide proton and nitrogen chemical shifts are often well approximated by a linear model, deviations from linearity are also observed and may be interpreted as evidence of fast exchange between distinct conformational states. Here, we describe computational methods, accessible via the Shift-T web server, including an automated tracking algorithm that propagates initial (single temperature)
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