Symmetry is a common theme in protein tertiary structure. The gene duplication and fusion hypothesis provides an evolutionary framework for the emergence of symmetric protein architectures from simpler peptide motifs; thus, evolutionary processes can guide de novo protein design. Utilization of symmetric principles in de novo protein design can also simplify the computational overhead substantially. An additional feature of symmetric protein architecture is the capacity for redundant folding nuclei – potentially enabling broad tolerance to mutation while retaining foldability. Symmetric protein architecture has been studied by experimental, theoretical, and computational scientists, and unique aspects relevant to protein evolution and design are emerging.
The goal of this research topic is to bring together, in a single resource, the most up-to-date experimental, theoretical and computational information and hypotheses related to the practical utilization of symmetry in de novo protein design. As a single step, de novo protein design has the challenging requirement of simultaneously solving at least three key problems, including 1) protein foldability (i.e., folding kinetics requirements), 2) protein stability (i.e., thermodynamic requirements), and 3) the accommodation of specific function (with potential structural dynamics requirements). These discrete design requirements are interconnected and likely orthogonal, as there is evidence for both “function/stability” and “function/foldability” tradeoffs. Protein design efforts can therefore benefit from the investigation of novel strategies to improve successful design outcomes, and the application of symmetric principles in protein design can potentially make a significant contribution. The current research topic thus aims to fulfill such an aim by inviting and publishing the best in class works by experimental, theoretical and computational investigators in this field. The platform will significantly motivate further research into this crucial area of protein science.
This Research Topic welcomes submissions of manuscripts including, but not limited to, the following topics:
• Evolution of symmetry in protein architecture
• Role of symmetry in protein folding
• Potential application of symmetric principles in de novo protein design
• Novel symmetry in protein architecture
• Utilization of symmetry in oligomerization of complex quaternary structure
• Understanding the functional universe available to symmetric protein architectures
• Computational and experimental tools for symmetric protein design
• Proteins with hitherto unreported symmetry and their function
• Biomedical applications of symmetry in protein architecture
• Novel materials applications of symmetric protein architecture
• Symmetry in protein-protein or protein-ligand interactions
• Protein symmetry applications in drug discovery and delivery
Prof. Michael Blaber is a cofounder of and has equity interest within the private company Trefoil Therapeutics Inc.
Symmetry is a common theme in protein tertiary structure. The gene duplication and fusion hypothesis provides an evolutionary framework for the emergence of symmetric protein architectures from simpler peptide motifs; thus, evolutionary processes can guide de novo protein design. Utilization of symmetric principles in de novo protein design can also simplify the computational overhead substantially. An additional feature of symmetric protein architecture is the capacity for redundant folding nuclei – potentially enabling broad tolerance to mutation while retaining foldability. Symmetric protein architecture has been studied by experimental, theoretical, and computational scientists, and unique aspects relevant to protein evolution and design are emerging.
The goal of this research topic is to bring together, in a single resource, the most up-to-date experimental, theoretical and computational information and hypotheses related to the practical utilization of symmetry in de novo protein design. As a single step, de novo protein design has the challenging requirement of simultaneously solving at least three key problems, including 1) protein foldability (i.e., folding kinetics requirements), 2) protein stability (i.e., thermodynamic requirements), and 3) the accommodation of specific function (with potential structural dynamics requirements). These discrete design requirements are interconnected and likely orthogonal, as there is evidence for both “function/stability” and “function/foldability” tradeoffs. Protein design efforts can therefore benefit from the investigation of novel strategies to improve successful design outcomes, and the application of symmetric principles in protein design can potentially make a significant contribution. The current research topic thus aims to fulfill such an aim by inviting and publishing the best in class works by experimental, theoretical and computational investigators in this field. The platform will significantly motivate further research into this crucial area of protein science.
This Research Topic welcomes submissions of manuscripts including, but not limited to, the following topics:
• Evolution of symmetry in protein architecture
• Role of symmetry in protein folding
• Potential application of symmetric principles in de novo protein design
• Novel symmetry in protein architecture
• Utilization of symmetry in oligomerization of complex quaternary structure
• Understanding the functional universe available to symmetric protein architectures
• Computational and experimental tools for symmetric protein design
• Proteins with hitherto unreported symmetry and their function
• Biomedical applications of symmetry in protein architecture
• Novel materials applications of symmetric protein architecture
• Symmetry in protein-protein or protein-ligand interactions
• Protein symmetry applications in drug discovery and delivery
Prof. Michael Blaber is a cofounder of and has equity interest within the private company Trefoil Therapeutics Inc.
