ArticleJournal of biological physics2014
THz time scale structural rearrangements and binding modes in lysozyme-ligand interactions.
Article in Journal of biological physics, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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8 citing papers in PubMed, 18 citations in OpenAlex.
- Thermally activated coupling between protein vibrations and interfacial water dynamics revealed by terahertz spectroscopy.iScience · 2026Article
- Quantum-topological simulation of Berry phase-induced fentanyl-μ-opioid receptor dissociation via terahertz vortex fields.Journal of molecular modeling · 2025Article
- Ultrafast terahertz-induced torque disruption of fentanyl's μ-opioid receptor binding for precision overdose reversal.Journal of molecular modeling · 2025Article
- Protein-Ligand Binding Molecular Details Revealed by Terahertz Optical Kerr Spectroscopy: A Simulation Study.JACS Au · 2021Article
- Equilibrium Ensembles for Insulin Folding from Bias-Exchange Metadynamics.Biophysical journal · 2017Article
- Vibrational resonance, allostery, and activation in rhodopsin-like G protein-coupled receptors.Scientific reports · 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
- The glassy state of crambin and the THz time scale protein-solvent fluctuations possibly related to protein function.BMC biophysics · 2014Article
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1 author at 1 institution in 1 country.
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Abstract
Predicting the conformational changes in proteins that are relevant for substrate binding is an ongoing challenge in the aim of elucidating the functional states of proteins. The motions that are induced by protein-ligand interactions are governed by the protein global modes. Our measurements indicate that the detected changes in the global backbone motion of the enzyme upon binding reflect a shift from the large-scale collective dominant mode in the unbound state towards a functional twisting deformation that assists in closing the binding cleft. Correlated motion in lysozyme has been implicated in enzyme function in previous studies, but detailed characterization of the internal fluctuations that enable the protein to explore the ensemble of conformations that ultimately foster large-scale conformational change is yet unknown. For this reason, we use THz spectroscopy to investigate the picosecond time scale binding modes and collective structural rearrangements that take place in hen egg white lysozyme (HEWL) when bound by the inhibitor (NAG)3. These protein thermal motions correspond to fluctuations that have a role in both selecting and sampling from the available protein intrinsic conformations that communicate function. Hence, investigation of these fast, collective modes may provide knowledge about the mechanism leading to the preferred binding process in HEWL-(NAG)3. Specifically, in this work we find that the picosecond time scale hydrogen-bonding rearrangements taking place in the protein hydration shell with binding modify the packing density within the hydrophobic core on a local level. These localized, intramolecular contact variations within the protein core appear to facilitate the large cooperative movements within the interfacial region separating the α- and β- domain that mediate binding. The THz time-scale fluctuations identified in the protein-ligand system may also reveal a molecular mechanism for substrate recognition.
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