ArticleBMC biophysics2014
The glassy state of crambin and the THz time scale protein-solvent fluctuations possibly related to protein function.
Article in BMC biophysics, 2014. 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.
- Hydration Contribution to the Solvation Free Energy of Water-Soluble Polymers.The journal of physical chemistry. B · 2025Article
- MACE-OFF: Short-Range Transferable Machine Learning Force Fields for Organic Molecules.Journal of the American Chemical Society · 2025Article
- Biomolecular dynamics with machine-learned quantum-mechanical force fields trained on diverse chemical fragments.Science advances · 2024Article
- Molecular Dynamics Simulation of the Influence of Temperature and Salt on the Dynamic Hydration Layer in a Model Polyzwitterionic Polymer PAEDAPS.The journal of physical chemistry. B · 2023Article
- New insights into the microscopic interactions associated with the physical mechanism of action of highly diluted biologics.Scientific reports · 2021Article
- THz Fingerprints of Cement-Based Materials.Materials (Basel, Switzerland) · 2020Article
- Conformational perturbation, allosteric modulation of cellular signaling pathways, and disease in P23H rhodopsin.Scientific reports · 2020Article
- Peptide-Protein Binding Investigated by Far-IR Spectroscopy and Molecular Dynamics Simulations.Biophysical journal · 2017Article
- Chlorophyll-Derivative Modulation of Rhodopsin Signaling Properties through Evolutionarily Conserved Interaction Pathways.Frontiers in molecular biosciences · 2017Article
- Vibrational resonance, allostery, and activation in rhodopsin-like G protein-coupled receptors.Scientific reports · 2016Article
- Elucidating the fundamental forces in protein crystal formation: the case of crambin.Chemical science · 2016Article
- Using THz Spectroscopy, Evolutionary Network Analysis Methods, and MD Simulation to Map the Evolution of Allosteric Communication Pathways in c-Type Lysozymes.Molecular biology and evolution · 2016Article
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1 author.
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Abstract
backgroundTHz experiments have been used to characterize the picosecond time scale fluctuations taking place in the model, globular protein crambin.
resultsUsing both hydration and temperature as an experimental parameter, we have identified collective fluctuations (<= 200 cm(-1)) in the protein. Observation of the protein dynamics in the THz spectrum from both below and above the glass transition temperature (Tg) has provided unique insight into the microscopic interactions and modes that permit the solvent to effectively couple to the protein thermal fluctuations.
conclusionsOur findings suggest that the solvent dynamics on the picosecond time scale not only contribute to protein flexibility but may also delineate the types of fluctuations that are able to form within the protein structure.
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