Research Topic

Protein Folding and Evolution: Information, Function and Disease

About this Research Topic

The structure/function link for proteins has for a long time served as a convenient paradigm. Increasing evidence suggests however that the order/disorder landscape in proteins is far more complex than hitherto imagined, and is an ongoing product of an exquisitely tuned evolutionary process. Furthermore, the field has been dominated by a restricted mindset resulting in neglected areas and unconventional concepts on the periphery of the main topic that we feel deserve to be addressed. Following on from the introduction of the concept of structural capacity and its inextricable origins in ribosome evolution, we wish to illustrate how transitions involving order/disorder rearrangements are involved not only in the selection of new folds and thus functions, but also play a role in the unavoidably associated increase in dysfunction and disease. The underlying theme will be the emergence of the role of information transfer between the genetic code repository and protein structure/function.

The number of potential protein folds and hence structures is immense. It is a sobering fact that the number of known folds is infinitesimally small compared to those potentially available. Current techniques, strongly influenced by main-stream structural biology approaches such as X-ray crystallography have described few of the protein structures that potentially could exist. The concept of evolutionary selection as an ongoing process, and the acceptance that proteins are dynamic structures lead to a reorganization of how the protein structure/function paradigm is viewed. The immense impact of molecular modelling, powered not only by huge computational capacities but also by machine learning and AI (Artificial Intelligence) algorithms is revolutionizing the whole field.
Our aim therefore, is to collate a series of original articles that address the relationship between protein structure and function from both an evolutionary and dynamic point of view. We aim to create a platform for launching new models based on original, innovative ideas or experimental approaches. The final goal is thus to seek and exploit hitherto unexplored facets of protein structure/function with the practical aim of facilitating protein engineering and expanding our knowledge of the origins and direction of life processes, with important impact on health issues.

Within the broad scope of protein evolution, we are seeking contributions on the following topics although this list is neither exhaustive nor exclusive:

• The evolution of protein folds and function;
• The role of order disorder transitions in protein evolution;
• The consequences of ribosomal evolution;
• Information theory, protein structure/function and evolution;
• Evolution, protein folding and disease;
• The inevitable link between evolved function and disease;
• The evolution of information transfer: from the genetic code to protein structure;
• Moonlighting proteins: disorder and order in multi-functional proteins;
• Protein Engineering and design: how to harness disorder?

Articles may be either data based novel observations, innovative technologies which grant new insights into protein dynamics or theoretical approaches that provide new testable models. We will be particularly attentive to “fringe ideas” independent of how unconventional they may be and welcome contributions from young unestablished scientists.


Dr. Ashley Buckle is founder of the structural biology and protein engineering company PTNG Consulting, and holds patents in the field. All other Topic Editors declare no competing interests.


Keywords: protein evolution, protein folding, protein engineering, intrinsically disordered proteins, protein folding evolution and disease


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.

The structure/function link for proteins has for a long time served as a convenient paradigm. Increasing evidence suggests however that the order/disorder landscape in proteins is far more complex than hitherto imagined, and is an ongoing product of an exquisitely tuned evolutionary process. Furthermore, the field has been dominated by a restricted mindset resulting in neglected areas and unconventional concepts on the periphery of the main topic that we feel deserve to be addressed. Following on from the introduction of the concept of structural capacity and its inextricable origins in ribosome evolution, we wish to illustrate how transitions involving order/disorder rearrangements are involved not only in the selection of new folds and thus functions, but also play a role in the unavoidably associated increase in dysfunction and disease. The underlying theme will be the emergence of the role of information transfer between the genetic code repository and protein structure/function.

The number of potential protein folds and hence structures is immense. It is a sobering fact that the number of known folds is infinitesimally small compared to those potentially available. Current techniques, strongly influenced by main-stream structural biology approaches such as X-ray crystallography have described few of the protein structures that potentially could exist. The concept of evolutionary selection as an ongoing process, and the acceptance that proteins are dynamic structures lead to a reorganization of how the protein structure/function paradigm is viewed. The immense impact of molecular modelling, powered not only by huge computational capacities but also by machine learning and AI (Artificial Intelligence) algorithms is revolutionizing the whole field.
Our aim therefore, is to collate a series of original articles that address the relationship between protein structure and function from both an evolutionary and dynamic point of view. We aim to create a platform for launching new models based on original, innovative ideas or experimental approaches. The final goal is thus to seek and exploit hitherto unexplored facets of protein structure/function with the practical aim of facilitating protein engineering and expanding our knowledge of the origins and direction of life processes, with important impact on health issues.

Within the broad scope of protein evolution, we are seeking contributions on the following topics although this list is neither exhaustive nor exclusive:

• The evolution of protein folds and function;
• The role of order disorder transitions in protein evolution;
• The consequences of ribosomal evolution;
• Information theory, protein structure/function and evolution;
• Evolution, protein folding and disease;
• The inevitable link between evolved function and disease;
• The evolution of information transfer: from the genetic code to protein structure;
• Moonlighting proteins: disorder and order in multi-functional proteins;
• Protein Engineering and design: how to harness disorder?

Articles may be either data based novel observations, innovative technologies which grant new insights into protein dynamics or theoretical approaches that provide new testable models. We will be particularly attentive to “fringe ideas” independent of how unconventional they may be and welcome contributions from young unestablished scientists.


Dr. Ashley Buckle is founder of the structural biology and protein engineering company PTNG Consulting, and holds patents in the field. All other Topic Editors declare no competing interests.


Keywords: protein evolution, protein folding, protein engineering, intrinsically disordered proteins, protein folding evolution and disease


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.

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