ArticleProceedings of the National Academy of Sciences of the United States of America2016
Computational investigation of cold denaturation in the Trp-cage miniprotein.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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21 citing papers in PubMed.
- Structural and functional dissection of human neurolysin through alanine-scanning mutagenesis.The FEBS journal · 2026Article
- Probabilistic Forecasting for Coarse-Grained Molecular Dynamics.Journal of chemical theory and computation · 2026Article
- Mechanism of lipid-dependent cold sensitivity in a model ion channel.Nature communications · 2026Article
- Temperature-dependent gating pathways in TRPV3.Scientific reports · 2026Article
- Mechanism Insights in Freeze-Thaw Process Impacting Cold Denaturation of Gluten Proteins During Frozen Storage.Foods (Basel, Switzerland) · 2025Article
- Impact of Dehydration Processing on Scallop (Foods (Basel, Switzerland) · 2025Article
- Nanocrystallites Modulate Intermolecular Interactions in Cryoprotected Protein Solutions.The journal of physical chemistry. B · 2023Article
- Coherent X-ray Scattering Reveals Nanoscale Fluctuations in Hydrated Proteins.The journal of physical chemistry. B · 2023Article
- Comparison of the Determination of Some Antihypertensive Drugs in Clinical Human Plasma Samples by Solvent Front Position Extraction and Precipitation Modes.Molecules (Basel, Switzerland) · 2023Article
- Reversible switching between two common protein folds in a designed system using only temperature.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Review
- Conformational Stability and Denaturation Processes of Proteins Investigated by Electrophoresis under Extreme Conditions.Molecules (Basel, Switzerland) · 2022Review
- Heat and cold denaturation of yeast frataxin: The effect of pressure.Biophysical journal · 2022Article
- From Protein Design to the Energy Landscape of a Cold Unfolding Protein.The journal of physical chemistry. B · 2022Article
- Insights into the effects of different drying methods on protein oxidation and degradation characteristics of golden pompano (Frontiers in nutrition · 2022Article
- Spatially resolved free-energy contributions of native fold and molten-globule-like Crambin.Biophysical journal · 2021Article
- An experimental approach probing the conformational transitions and energy landscape of antibodies: a glimmer of hope for reviving lost therapeutic candidates using ionic liquid.Chemical science · 2021Article
- Behavior of Proteins under Pressure from Experimental Pressure-Dependent Structures.The journal of physical chemistry. B · 2021Article
- Hydration shell differentiates folded and disordered states of a Trp-cage miniprotein, allowing characterization of structural heterogeneity by wide-line NMR measurements.Scientific reports · 2019Article
- Cryo-Cooling Effect on DHFR Crystal Studied by Replica-Exchange Molecular Dynamics Simulations.Biophysical journal · 2019Article
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3 authors.
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Abstract
The functional native states of globular proteins become unstable at low temperatures, resulting in cold unfolding and impairment of normal biological function. Fundamental understanding of this phenomenon is essential to rationalizing the evolution of freeze-tolerant organisms and developing improved strategies for long-term preservation of biological materials. We present fully atomistic simulations of cold denaturation of an α-helical protein, the widely studied Trp-cage miniprotein. In contrast to the significant destabilization of the folded structure at high temperatures, Trp-cage cold denatures at 210 K into a compact, partially folded state; major elements of the secondary structure, including the α-helix, are conserved, but the salt bridge between aspartic acid and arginine is lost. The stability of Trp-cage's α-helix at low temperatures suggests a possible evolutionary explanation for the prevalence of such structures in antifreeze peptides produced by cold-weather species, such as Arctic char. Although the 310-helix is observed at cold conditions, its position is shifted toward Trp-cage's C-terminus. This shift is accompanied by intrusion of water into Trp-cage's interior and the hydration of buried hydrophobic residues. However, our calculations also show that the dominant contribution to the favorable energetics of low-temperature unfolding of Trp-cage comes from the hydration of hydrophilic residues.
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