ArticleJournal of biomolecular NMR2007
Complexity of aromatic ring-flip motions in proteins: Y97 ring dynamics in cytochrome c observed by cross-relaxation suppressed exchange NMR spectroscopy.
Article in Journal of biomolecular NMR, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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11 citing papers in PubMed, 25 citations in OpenAlex.
- Genetically Encoded Pentafluorophenylalanine Enables Quantitative Probing of Local Protein Malleability by 19F NMR.Journal of the American Chemical Society · 2026Article
- Free-Energy Landscape and Rate Estimation of the Aromatic Ring Flips in Basic Pancreatic Trypsin Inhibitors Using Metadynamics.Journal of chemical theory and computation · 2023Article
- NMR Studies of Aromatic Ring Flips to Probe Conformational Fluctuations in Proteins.The journal of physical chemistry. B · 2023Review
- Article
- Transition-State Compressibility and Activation Volume of Transient Protein Conformational Fluctuations.JACS Au · 2021Article
- Discriminating changes in protein structure using tyrosine conjugation.Protein science : a publication of the Protein Society · 2020Article
- Dynamics of Hydrophobic Core Phenylalanine Residues Probed by Solid-State Deuteron NMR.The journal of physical chemistry. B · 2015Article
- Off-resonance rotating-frame relaxation dispersion experiment for 13C in aromatic side chains using L-optimized TROSY-selection.Journal of biomolecular NMR · 2014Article
- Tyrosine phosphorylation turns alkaline transition into a biologically relevant process and makes human cytochrome c behave as an anti-apoptotic switch.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2011Article
- Structure, dynamics, and ionization equilibria of the tyrosine residues in Bacillus circulans xylanase.Journal of biomolecular NMR · 2011Article
- Entropic stabilization of myoglobin by subdenaturing concentrations of guanidine hydrochloride.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2009Article
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2 authors at 1 institution in 1 country.
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Abstract
Dynamics of large-amplitude conformational motions in proteins are complex and less understood, although these processes are intimately associated with structure, folding, stability, and function of proteins. Here, we use a large set of spectra obtained by cross-relaxation suppressed exchange NMR spectroscopy (EXSY) to study the 180 degrees flipping motion of the Y97 ring of horse ferricytochrome c as a function of near-physiological temperature in the 288-308 K range. With rising temperature, the ring-flip rate constant makes a continuous transition from Arrhenius to anti-Arrhenius behavior through a narrow Arrhenius-like zone. This behavior is seen not only for the native state of the protein, but also for native-like states generated by adding subdenaturing amounts of guanidine deuterochloride (GdnDCl). Moderately destabilizing concentrations of the denaturant (1.5 M GdnDCl) completely removes the Arrhenius-like feature from the temperature window employed. The Arrhenius to anti-Arrhenius transition can be explained by the heat capacity model where temperature strengthens ground state interactions, perhaps hydrophobic in nature. The effect of the denaturant may appear to arise from direct protein-denaturant interactions that are structure-stabilizing under subdenaturing conditions. The temperature distribution of rate constants under different stability conditions also suggests that the prefactor in Arrhenius-like relations is temperature dependent. Although the use of the transition state theory (TST) offers several challenges associated with data interpretation, the present results and a consideration of others published earlier provide evidence for complexity of ring-flip dynamics in proteins.
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