About this Research Topic
Unraveling the mechanistic details of protein function is essential to furthering efforts in bioengineering, precision medicine, and drug discovery. However, many of the most attractive protein targets have large scaffolds with multiple ligand binding sites or vast conformational equilibria. Many of these systems utilize allostery, the transmission of chemical information between spatially distinct regions of the protein, as a regulatory mechanism. However, allostery itself is poorly understood, hampering our ability to reconcile novel biological findings with classical paradigms.
A “holy grail” of biophysical chemistry has been to understand how ligand binding information is transmitted through a protein matrix to induce a functional response. The pathways most critical to the flow of chemical information are often intimately linked with the conformational ensembles populated by biomolecules and spatially distant from traditional catalytic or ligand binding sites. In order to harness the potential of allosteric regulation to provide enhanced spatial and temporal control of protein function, the mechanistic details of these challenging protein targets must be established. Recent advances in spectroscopy, electron microscopy, and molecular simulations have facilitated synergistic investigations of protein structure and dynamics aimed at mapping dynamic pathways that underlie long-range allosteric communication.
We welcome Original Research Articles and Reviews discussing recent advances in the biophysical characterization and mechanistic understanding of protein function, including the influence of conformational dynamics, allostery, and molecular interactions. Presentation of synergistic experimental-computational studies or multi-disciplinary spectroscopic studies are welcome.
This Research Topic will cover, but is not limited to, the following areas:
• Solution studies of protein structure and dynamics
• Molecular simulations of functional pathways in proteins
• Mapping allosteric regulatory networks in complex systems
• Structural studies of protein-ligand (i.e. drugs, inhibitors, activators) or protein-protein interactions
• Molecular resolution of enzyme mechanisms
A “holy grail” of biophysical chemistry has been to understand how ligand binding information is transmitted through a protein matrix to induce a functional response. The pathways most critical to the flow of chemical information are often intimately linked with the conformational ensembles populated by biomolecules and spatially distant from traditional catalytic or ligand binding sites. In order to harness the potential of allosteric regulation to provide enhanced spatial and temporal control of protein function, the mechanistic details of these challenging protein targets must be established. Recent advances in spectroscopy, electron microscopy, and molecular simulations have facilitated synergistic investigations of protein structure and dynamics aimed at mapping dynamic pathways that underlie long-range allosteric communication.
We welcome Original Research Articles and Reviews discussing recent advances in the biophysical characterization and mechanistic understanding of protein function, including the influence of conformational dynamics, allostery, and molecular interactions. Presentation of synergistic experimental-computational studies or multi-disciplinary spectroscopic studies are welcome.
This Research Topic will cover, but is not limited to, the following areas:
• Solution studies of protein structure and dynamics
• Molecular simulations of functional pathways in proteins
• Mapping allosteric regulatory networks in complex systems
• Structural studies of protein-ligand (i.e. drugs, inhibitors, activators) or protein-protein interactions
• Molecular resolution of enzyme mechanisms
Keywords: NMR, cryo-EM, molecular dynamics, allostery, multidomain proteins, signaling, structural biology
Important Note: All contributions to this Research Topic must be within the scope of the section and journal to which they are submitted, as defined in their mission statements. Frontiers reserves the right to guide an out-of-scope manuscript to a more suitable section or journal at any stage of peer review.
