About this Research Topic
Louis Sullivan (1856 - 1924) revolutionized architecture by designing the first skyscraper, but he also became famous by proclaiming that “form follows function”. When x-ray crystallographers could have the first look at the structures of DNA and proteins, the structural biology field embraced the view that “function follows form”. Visualization of the 3D-architecture of proteins could unveil various aspects of protein function.
Yet, our current understanding has shifted from the original relationship of “1 gene - 1 protein structure - 1 function” to a far more complicated picture where the flexibility and dynamics of an individual protein can play a central role in a multitude of functions. The ultimate forms that a protein adopt when interacting with (a) partner molecule(s) are the most biologically relevant and in this context Sullivan’s quote is appropriate: the conFORMation that the protein adopts follows from the function of that protein.
Despite the fact that many well-characterized proteins have a well-folded structure, there is growing number of (partially) intrinsically disordered proteins with an emerging picture whereby conformational flexibility gains importance. Yet, flexibility is also a balanced phenomenon: excess of flexibility can be detrimental for protein behavior, as well as the lack of flexibility. Therefore, flexibility can be perceived as a friend or a foe, depending on the context.
The scope of this research topic is to cover in a balanced way the impact of the study of protein flexibility on the structural biology field and to raise the profile of protein flexibility to a broad audience. We would like to present protein flexibility in the context of disease as well as the benign aspects of flexibility. Allostery is such an example whereby the binding of a metabolic molecule can modify the structure and activity of an enzyme and thus finetune its function. On the other hand various IDPs are inherently linked to devastating medical conditions like cancer and neurodegenerative diseases. Besides comprehensively understanding protein flexibility, one of the future challenges for structural biology also lies with large macromolecular protein complexes. There the dynamics and flexibility are essential for proper functioning and molecular movement, which is an important aspect of living matter.
Detailed knowledge of the structural aspects of polypeptides remains essential to comprehend protein function. Besides mounting in vitro data, it remains a challenge to understand the in vivo behavior of protein flexibility and dynamics. This challenge stimulates us to develop advanced techniques to study protein flexibility and employ those techniques to address fundamental biological and biomedical problems. Those innovations should help us to unravel the intimate link between protein function and flexibility and explore new horizons.
In an editorial comment article, we intend to introduce the F3 concept: “form follows function” + “flexibility facilitates function” + “Form and function follow frequency (NMR)”
Yet, our current understanding has shifted from the original relationship of “1 gene - 1 protein structure - 1 function” to a far more complicated picture where the flexibility and dynamics of an individual protein can play a central role in a multitude of functions. The ultimate forms that a protein adopt when interacting with (a) partner molecule(s) are the most biologically relevant and in this context Sullivan’s quote is appropriate: the conFORMation that the protein adopts follows from the function of that protein.
Despite the fact that many well-characterized proteins have a well-folded structure, there is growing number of (partially) intrinsically disordered proteins with an emerging picture whereby conformational flexibility gains importance. Yet, flexibility is also a balanced phenomenon: excess of flexibility can be detrimental for protein behavior, as well as the lack of flexibility. Therefore, flexibility can be perceived as a friend or a foe, depending on the context.
The scope of this research topic is to cover in a balanced way the impact of the study of protein flexibility on the structural biology field and to raise the profile of protein flexibility to a broad audience. We would like to present protein flexibility in the context of disease as well as the benign aspects of flexibility. Allostery is such an example whereby the binding of a metabolic molecule can modify the structure and activity of an enzyme and thus finetune its function. On the other hand various IDPs are inherently linked to devastating medical conditions like cancer and neurodegenerative diseases. Besides comprehensively understanding protein flexibility, one of the future challenges for structural biology also lies with large macromolecular protein complexes. There the dynamics and flexibility are essential for proper functioning and molecular movement, which is an important aspect of living matter.
Detailed knowledge of the structural aspects of polypeptides remains essential to comprehend protein function. Besides mounting in vitro data, it remains a challenge to understand the in vivo behavior of protein flexibility and dynamics. This challenge stimulates us to develop advanced techniques to study protein flexibility and employ those techniques to address fundamental biological and biomedical problems. Those innovations should help us to unravel the intimate link between protein function and flexibility and explore new horizons.
In an editorial comment article, we intend to introduce the F3 concept: “form follows function” + “flexibility facilitates function” + “Form and function follow frequency (NMR)”
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