ArticleJACS Au2021
Transition-State Compressibility and Activation Volume of Transient Protein Conformational Fluctuations.
Article in JACS Au, 2021. 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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Who cites it
11 citing papers in PubMed.
- 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
- Molecular neighbours reshape protein dynamics.Nature chemistry · 2026Article
- Aromatic ring flips reveal reshaping of protein dynamics in crystals and complexes.Nature chemistry · 2026Article
- 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
- Incorporating the thermodynamic effects of temperature and pressure on modeling neuronal gating kinetics.PloS one · 2025Article
- 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
- High Pressure CPMG and CEST Reveal That Cavity Position Dictates Distinct Dynamic Disorder in the PP32 Repeat Protein.The journal of physical chemistry. B · 2022Article
- 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
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Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Proteins are dynamic entities that intermittently depart from their ground-state structures and undergo conformational transitions as a critical part of their functions. Central to understanding such transitions are the structural rearrangements along the connecting pathway, where the transition state plays a special role. Using NMR relaxation at variable temperature and pressure to measure aromatic ring flips inside a protein core, we obtain information on the structure and thermodynamics of the transition state. We show that the isothermal compressibility coefficient of the transition state is similar to that of short-chain hydrocarbon liquids, implying extensive local unfolding of the protein. Our results further indicate that the required local volume expansions of the protein can occur not only with a net positive activation volume of the protein, as expected from previous studies, but also with zero activation volume by compaction of remote void volume, when averaged over the ensemble of states.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.