About this Research Topic
The expanding horizons of machine learning has enabled reasoning over and systematic learning of 3D atomic coordinates of proteins structures to create an empirical map with their corresponding
amino acid sequences. This has since opened up a gamut of possibilities to better understand why and how a sequence of contiguously strung amino acids fold into a particular geometric shape. While the unified rules of protein folding still remains elusive, efforts geared towards understanding protein-ligand, protein-protein interactions have been able to tap into hitherto unknown biology. Being able to predict inter-residue distances in a target protein, or between a ligand and a protein with high fidelity has been the central objective to such endeavors.
Proteins that lack similarity with other natural proteins such as de novo proteins, and rapidly evolving viral sequences remain the hardest to be predicted. Any progress towards discerning biophysics of novel protein interactions, exploring degenerate conformational geometries of the same protein (allostery), or methods to glean key residue-residue contacts that control protein shape – will constitute extremely important reads in this space of science.
To illustrate for the readers of ‘Frontiers of Bioengineering and Biotechnology’ in general, the Research Topic titled “Advances in Protein Structure, Function, and Design” within the journal’s
scope of ‘Bioprocess Engineering’, is intended to present several aspects of discerning the fundamentals of protein structure and protein interactions.
We encourage the submission of research papers that focus on but are not limited to, the following
themes:
• Protein-protein/ protein-ligand interactions
• Protein structure-function mapping
• Protein structure prediction
• Protein design
• Peptide-based biomaterials
• Enzyme Engineering
We look forward to reading your contributions for this Research Topic.
amino acid sequences. This has since opened up a gamut of possibilities to better understand why and how a sequence of contiguously strung amino acids fold into a particular geometric shape. While the unified rules of protein folding still remains elusive, efforts geared towards understanding protein-ligand, protein-protein interactions have been able to tap into hitherto unknown biology. Being able to predict inter-residue distances in a target protein, or between a ligand and a protein with high fidelity has been the central objective to such endeavors.
Proteins that lack similarity with other natural proteins such as de novo proteins, and rapidly evolving viral sequences remain the hardest to be predicted. Any progress towards discerning biophysics of novel protein interactions, exploring degenerate conformational geometries of the same protein (allostery), or methods to glean key residue-residue contacts that control protein shape – will constitute extremely important reads in this space of science.
To illustrate for the readers of ‘Frontiers of Bioengineering and Biotechnology’ in general, the Research Topic titled “Advances in Protein Structure, Function, and Design” within the journal’s
scope of ‘Bioprocess Engineering’, is intended to present several aspects of discerning the fundamentals of protein structure and protein interactions.
We encourage the submission of research papers that focus on but are not limited to, the following
themes:
• Protein-protein/ protein-ligand interactions
• Protein structure-function mapping
• Protein structure prediction
• Protein design
• Peptide-based biomaterials
• Enzyme Engineering
We look forward to reading your contributions for this Research Topic.
Keywords: Protein Interactions, Protein Structure and folding, Protein Function, Protein Engineering, Protein-based biomaterials, Peptide-based biosensors, Biomolecular simulations
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.
