ArticleProceedings of the National Academy of Sciences of the United States of America2017
Critical structural fluctuations of proteins upon thermal unfolding challenge the Lindemann criterion.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed.
- Cytoplasmic fluidity and the cold life: proteome stability is decoupled from viability in psychrophiles.Nature communications · 2025Article
- Microscopic versus Macroscopic Glass Transitions and Relevant Length Scales in Mixtures of Industrial Interest.Macromolecules · 2023Article
- Polymorphism and Ligand Binding Modulate Fast Dynamics of Human Telomeric G-Quadruplexes.International journal of molecular sciences · 2023Article
- Thermal Stability Estimation of Single Domain Antibodies Using Molecular Dynamics Simulations.Methods in molecular biology (Clifton, N.J.) · 2023Article
- Protein Dynamics to Define and Refine Disordered Protein Ensembles.The journal of physical chemistry. B · 2022Article
- Computational Insights into the Unfolding of a Destabilized Superoxide Dismutase 1 Mutant.Biology · 2021Article
- A Minireview on Temperature Dependent Protein Conformational Sampling.The protein journal · 2021Review
- The number of catalytic cycles in an enzyme's lifetime and why it matters to metabolic engineering.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Configurational Entropy of Folded Proteins and Its Importance for Intrinsically Disordered Proteins.International journal of molecular sciences · 2021Article
- Rapid Characterization of Biomolecules' Thermal Stability in a Segmented Flow-Through Optofluidic Microsystem.Scientific reports · 2020Article
- Thermal stability of single-domain antibodies estimated by molecular dynamics simulations.Protein science : a publication of the Protein Society · 2019Article
- Determination of Dynamical Heterogeneity from Dynamic Neutron Scattering of Proteins.Biophysical journal · 2018Article
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8 authors.
Funding
Abstract
Internal subnanosecond timescale motions are key for the function of proteins, and are coupled to the surrounding solvent environment. These fast fluctuations guide protein conformational changes, yet their role for protein stability, and for unfolding, remains elusive. Here, in analogy with the Lindemann criterion for the melting of solids, we demonstrate a common scaling of structural fluctuations of lysozyme protein embedded in different environments as the thermal unfolding transition is approached. By combining elastic incoherent neutron scattering and advanced molecular simulations, we show that, although different solvents modify the protein melting temperature, a unique dynamical regime is attained in proximity of thermal unfolding in all solvents that we tested. This solvation shell-independent dynamical regime arises from an equivalent sampling of the energy landscape at the respective melting temperatures. Thus, we propose that a threshold for the conformational entropy provided by structural fluctuations of proteins exists, beyond which thermal unfolding is triggered.
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