Editorial |
Message from the Editors
Here we inaugurate our first special targeted issue of PEDS, in this case on protein folding. We are pleased with the response of our editorial board to contribute to this volume. We anticipate future special issues on antibodies, membrane proteins, computational methods, protein design, protein aggregation, and biotechnological applications. Again we will be appealing to our board members to provide material, which, as with this volume, will be peer reviewed. However, we will also advertise upcoming volumes in advance on our website so that others in the community can contribute.This volume of protein folding contains mainly experimental papers addressing the pathway of folding and characterization of species en route. That said, protein engineering and design are critical to virtually all of the studies contained in this volume. Fersht and co-workers carefully analyze the burst phase of the FF domain, a small helical protein, showing that it populates a robust folding intermediate, which provides further support for their earlier studies of this protein. In another contribution, the Fersht group revisits the folding of another small helical protein—the engrailed homeodomain. In this case they complement the vast amount of information on the folding pathway of this protein with fluorescence resonance energy transfer data. Regan and co-workers (van Nuland et al.) also revisit the folding behavior of one of their favorite proteins—Rop, a four-helix bundle protein. Here they describe real-time NMR studies to detect and further characterize the intermediate. Then, in a separate submission Regan and co-workers (Dalal et al.) describe studies of three naturally occurring Rop homologues. Although these proteins have different stabilities and folding rates, they share similar mechanisms of folding/unfolding. The determinants of stability are addressed in great detail for a small model system—the designed Trp-cage miniprotein by Andersen and co-workers.
Several papers address the consequences and mechanism of misfolding. Daggett and co-workers describe how different human disease-causing mutations in transthyretin trigger the same conformational change, which in turn is implicated in amyloidosis. Miranker and co-workers move further along the amyloidosis pathway to describe the fibrillar assembly of the islet amyloid polypeptide. Finally, Murphy and co-workers describe an approach for systematically generating libraries of polyglutamine of different lengths in model host proteins. Polyglutamine expansions are implicated in many neurodegenerative diseases and this study provides the basis for detailed investigations of the relationship between polyglutamine length, context, misfolding and aggregation.
While the studies described in this issue utilize protein engineering and design principles to shed light on folding and misfolding processes, a better understanding of the fundamentals of protein folding is also critical for many engineering and design applications.
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