ArticleProtein science : a publication of the Protein Society2004
Infrequent cavity-forming fluctuations in HPr from Staphylococcus carnosus revealed by pressure- and temperature-dependent tyrosine ring flips.
Article in Protein science : a publication of the Protein Society, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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27 citing papers in PubMed, 50 citations in OpenAlex.
- Genetically Encoded Pentafluorophenylalanine Enables Quantitative Probing of Local Protein Malleability by 19F NMR.Journal of the American Chemical Society · 2026Article
- Pressure-Dependent Aromatic Ring Flips Reveal Variable Transition-State Volume and Compressibility Among Structural Regions of BPTI.Chembiochem : a European journal of chemical biology · 2026Article
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- Changes in the Aqueous Solvent do not Impact the Internal Ring-Flip Dynamic of Fully Buried F52 in Protein GB1.Chembiochem : a European journal of chemical biology · 2025Article
- 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
- Effect of Cross-Seeding of Wild-Type Amyloid-βThe journal of physical chemistry. B · 2023Article
- NMR Studies of Aromatic Ring Flips to Probe Conformational Fluctuations in Proteins.The journal of physical chemistry. B · 2023Review
- Aromatic ring flips in differently packed ubiquitin protein crystals from MAS NMR and MD.Journal of structural biology: X · 2023Article
- Characterizing Fast Conformational Exchange of Aromatic Rings Using Residual Dipolar Couplings: Distinguishing Jumplike Flips from Other Exchange Mechanisms.The journal of physical chemistry. B · 2022Article
- Comparative Hydrophobic Core Dynamics Between Wild-Type Amyloid-β Fibrils, Glutamate-3 Truncation, and Serine-8 Phosphorylation.Chemphyschem : a European journal of chemical physics and physical chemistry · 2022Article
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- Transition-State Compressibility and Activation Volume of Transient Protein Conformational Fluctuations.JACS Au · 2021Article
- Pepsin-like aspartic proteases (PAPs) as model systems for combining biomolecular simulation with biophysical experiments.RSC advances · 2021Review
- Slow ring flips in aromatic cluster of GB1 studied by aromaticJournal of biomolecular NMR · 2020Article
- Aromatic Ring Dynamics, Thermal Activation, and Transient Conformations of a 468 kDa Enzyme by SpecificJournal of the American Chemical Society · 2019Article
- Practical aspects of high-pressure NMR spectroscopy and its applications in protein biophysics and structural biology.Methods (San Diego, Calif.) · 2018Article
- Solvent-Driven Dynamical Crossover in the Phenylalanine Side-Chain from the Hydrophobic Core of Amyloid Fibrils Detected byThe journal of physical chemistry. B · 2017Article
- Finding Our Way in the Dark Proteome.Journal of the American Chemical Society · 2016Article
- Dynamics of Hydrophobic Core Phenylalanine Residues Probed by Solid-State Deuteron NMR.The journal of physical chemistry. B · 2015Article
- A sharp thermal transition of fast aromatic-ring dynamics in ubiquitin.Angewandte Chemie (International ed. in English) · 2015Article
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Authors and funding
7 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Infrequent structural fluctuations of a globular protein is seldom detected and studied in detail. One tyrosine ring of HPr from Staphylococcus carnosus, an 88-residue phosphocarrier protein with no disulfide bonds, undergoes a very slow ring flip, the pressure and temperature dependence of which is studied in detail using the on-line cell high-pressure nuclear magnetic resonance technique in the pressure range from 3 MPa to 200 MPa and in the temperature range from 257 K to 313 K. The ring of Tyr6 is buried sandwiched between a beta-sheet and alpha-helices (the water-accessible area is less than 0.26 nm2), its hydroxyl proton being involved in an internal hydrogen bond. The ring flip rates 10(1)-10(5) s(-1) were determined from the line shape analysis of H(delta1, delta2) and H(epsilon1,epsilon2) of Tyr6, giving an activation volume DeltaV++ of 0.044 +/- 0.008 nm3 (27 mL mol(-1)), an activation enthalpy DeltaH++ of 89 +/- 10 kJ mol(-1), and an activation entropy DeltaS++ of 16 +/- 2 JK(-1) mol(-1). The DeltaV++) and DeltaH++ values for HPr found previously for Tyr and Phe ring flips of BPTI and cytochrome c fall within the range of DeltaV(double dagger) of 28 to 51 mL mol(-1) and DeltaH++ of 71 to 155 kJ mol(-1). The fairly common DeltaV++ and DeltaH++ values are considered to represent the extra space or cavity required for the ring flip and the extra energy required to create a cavity, respectively, in the core part of a globular protein. Nearly complete cold denaturation was found to take place at 200 MPa and 257 K independently from the ring reorientation process.
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