ArticleNature communications2017
Molecular determinant of the effects of hydrostatic pressure on protein folding stability.
Article in Nature communications, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.
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Who cites it
38 citing papers in PubMed, 114 citations in OpenAlex.
- Unveiling Van Der Waals Forces and Associated Hamaker Constants Across the Nanomaterial Landscape With Advanced Atomic Force Microscopy.Small methods · 2026Review
- Functionally related internal fluctuations in human ileal bile acid-binding protein by high pressure nuclear magnetic resonance.Protein science : a publication of the Protein Society · 2026Article
- Effect of high hydrostatic pressure on D-amino acid oxidase activity and stability.Journal of biological engineering · 2026Article
- Role of vinculin in the structural dynamics of cadherin-catenin complexes and its implications for F-actin binding.Protein science : a publication of the Protein Society · 2025Article
- Probing Contributions to the Volume and Isothermal Compressibility of Globular Proteins Using a Fluctuation Solution Theory Analysis of MD Simulations.The journal of physical chemistry. B · 2025Article
- Pressure Protein Denaturation Compared to Thermal and Chemical Unfolding: Analyses with Cooperative Models.The journal of physical chemistry. B · 2025Article
- Computation suggests that the cell adhesion sub-proteome is enriched for sites of pH-dependence and charge burial.PloS one · 2025Article
- Characteristics of kidney stone-modulatory proteins decoded from proteins identified in stone matrix and urine of stone formers and non-stone subjects.Computational and structural biotechnology journal · 2025Article
- Regulation of gene expression under high hydrostatic pressure: the versatile role of the master regulator SurR in energy metabolism.Frontiers in microbiology · 2025Article
- Thermodynamic Origin of the Linear Pressure Dependence of DNA Thermal Stability.The journal of physical chemistry letters · 2024Article
- Destabilization of the D2 domain of Thermotoga maritima arginine binding protein induced by guanidinium thiocyanate and its counteraction by stabilizing agents.Protein science : a publication of the Protein Society · 2024Article
- Article
- On the Stabilizing Effect of Aspartate and Glutamate and Its Counteraction by Common Denaturants.International journal of molecular sciences · 2024Article
- Protein Stability─Analysis of Heat and Cold Denaturation without and with Unfolding Models.The journal of physical chemistry. B · 2023Article
- Strategy for the Adaptation to Stressful Conditions of the Novel Isolated Conditional Piezophilic Strain Halomonas titanicae ANRCS81.Applied and environmental microbiology · 2023Article
- The volume changes of unfolding of dsDNA.Biophysical journal · 2022Article
- Understanding Primary Blast Injury: High Frequency Pressure Acutely Disrupts Neuronal Network Dynamics in Cerebral Organoids.Journal of neurotrauma · 2022Article
- Mechanical Stability of Ribonuclease A Heavily Depends on the Redox Environment.The journal of physical chemistry. B · 2022Article
- Decoding the Effect of Hydrostatic Pressure on TRPV1 Lower-Gate Conformation by Molecular-Dynamics Simulation.International journal of molecular sciences · 2022Article
- Exploration of the dynamic interplay between lipids and membrane proteins by hydrostatic pressure.Nature communications · 2022Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Hydrostatic pressure is an important environmental variable that plays an essential role in biological adaptation for many extremophilic organisms (for example, piezophiles). Increase in hydrostatic pressure, much like increase in temperature, perturbs the thermodynamic equilibrium between native and unfolded states of proteins. Experimentally, it has been observed that increase in hydrostatic pressure can both increase and decrease protein stability. These observations suggest that volume changes upon protein unfolding can be both positive and negative. The molecular details of this difference in sign of volume changes have been puzzling the field for the past 50 years. Here we present a comprehensive thermodynamic model that provides in-depth analysis of the contribution of various molecular determinants to the volume changes upon protein unfolding. Comparison with experimental data shows that the model allows quantitative predictions of volume changes upon protein unfolding, thus paving the way to proteome-wide computational comparison of proteins from different extremophilic organisms.
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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.