Protein Folding Intermediates: From Guiding Proper Folding to Human Diseases and Clinical Viewpoints

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About this Research Topic

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Background

Proper protein folding is a very crucial event in the cell. Any shortcomings in such protein-folding pathways result in the production of misfolded or toxic protein species. In recent decades there has been significant progress in understanding the protein folding landscape, including pathways, kinetics, thermodynamics, etc. Several protein folding enhancing chaperones, co-chaperones, chaperone complexes, and folding mechanisms have also been unveiled. One important landmark development in protein folding is that folding proceeds via the formation of folding intermediates. It is believed that folding intermediates determine the structure of the native state of the protein. Nowadays folding intermediates have been given obvious attention because of the fact that these intermediates are the stepping-stones to large number of human diseases, including Parkinson’s, multiple systemic atrophy, Alzheimer’s etc. Several on-pathway, off-pathway intermediates and aggregation-prone species have been explored to date. Consequently rationality toward their association with human diseases is being established.

In order to design an appropriate stratagem of targeting protein folding intermediates toward the therapeutic intervention of protein misfolding-linked human diseases, a comprehensive knowledge on the structural, and functional aspects of different intermediates and their roles in modulating the folding landscape is essential. Despite developments in understanding how the folding intermediates assist to maintain the fidelity of protein folding process, the nature and role of folding intermediates in causing protein misfolding and/or consequent disease development have been the topic of much heated debate. More information is required on the nature, characteristics and heterogeneity of the folding intermediates in different protein families or types. Of particular interest is how differences in structural characteristics of an intermediate result in different protein folding/misfolding behavior, and a clear understanding here is yet to be established.

The goal of this Research Topic is to publish the most recent developments in protein folding intermediates, mechanistic data on how the intermediates help to induce the final native conformation, and their associations with human diseases. Cutting edge methodologies used to characterize folding intermediates, and their structural fluctuations, will also be included. Special focus will also be given to disease-linked mutant protein folding, the intermediates formed, and strategies to achieve their functional restoration. The Research Topic will not be limited to full original articles but also include, reviews, mini reviews, reports, case reports etc.

This Research Topic will cover articles related to the following sub themes:
• Studies on small molecule drugs that can alter the protein folding landscape
• Studies aimed at developing specific inhibitors of aggregation prone species (APS) and other kinetic intermediates
• Studies that address new insights to the protein folding pathway
• Detailed structural characteristics of new folding intermediates
• Cutting edge techniques used in understanding protein folding
• Mechanistic studies on the restoration of the function of disease-linked mutant proteins

Keywords: : Protein folding, Folding intermediates, protein aggregation, folding pathway, Amyloids, protein misfolding, molten globule state, mutant protein

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