ArticleJournal of biomolecular NMR2013
The protein amide ¹H(N) chemical shift temperature coefficient reflects thermal expansion of the N-H···O=C hydrogen bond.
Article in Journal of biomolecular NMR, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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12 citing papers in PubMed.
- Mesostructured Water Enhances Stability of ProteinMPNN-Designed Ubiquitin-Fold Proteins.Journal of the American Chemical Society · 2026Article
- The Temperature Dependence of Hydrogen Bonds Is More Uniform in Stable Proteins: An Analysis of NMRMolecules (Basel, Switzerland) · 2024Article
- NMR detection and conformational dependence of two, three, and four-bond isotope shifts due to deuteration of backbone amides.Journal of biomolecular NMR · 2023Article
- Destabilization of polar interactions in the prion protein triggers misfolding and oligomerization.Protein science : a publication of the Protein Society · 2021Article
- Biophysical and Dynamic Characterization of Fine-Tuned Binding of the Human Respiratory Syncytial Virus M2-1 Core Domain to Long RNAs.Journal of virology · 2020Article
- A Second Backbone: The Contribution of a Buried Asparagine Ladder to the Global and Local Stability of a Leucine-Rich Repeat Protein.Biochemistry · 2019Article
- Decreased conformational stability in the oncogenic N92I mutant of Ras-related C3 botulinum toxin substrate 1.Science advances · 2019Article
- UsingProtein science : a publication of the Protein Society · 2018Article
- Stability of Protein-Specific Hydration Shell on Crowding.Journal of the American Chemical Society · 2016Article
- Mechanism of Protein Denaturation: Partial Unfolding of the P22 Coat Protein I-Domain by Urea Binding.Biophysical journal · 2015Article
- Protein apparent dielectric constant and its temperature dependence from remote chemical shift effects.Journal of the American Chemical Society · 2014Article
- Impact of hydrostatic pressure on an intrinsically disordered protein: a high-pressure NMR study of α-synuclein.Chembiochem : a European journal of chemical biology · 2013Article
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3 authors.
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Abstract
The protein amide (1)H(N) chemical shift temperature coefficient can be determined with high accuracy by recording spectra at different temperatures, but the physical mechanism responsible for this temperature dependence is not well understood. In this work, we find that this coefficient strongly correlates with the temperature coefficient of the through-hydrogen-bond coupling, (3h)J(NC'), based on NMR measurements of protein GB3. Parallel tempering molecular dynamics simulation suggests that the hydrogen bond distance variation at different temperatures/replicas is largely responsible for the (1)H(N) chemical shift temperature dependence, from which an empirical equation is proposed to predict the hydrogen bond thermal expansion coefficient, revealing responses of individual hydrogen bonds to temperature changes. Different expansion patterns have been observed for various networks formed by β strands.
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