The art of paper folding is a useful way to illustrate some concepts about protein folding in the cell, according to June’s issue of Nature Structural and Molecular Biology. “When all goes well, you end up with a beautiful and functional structure. When things go wrong (misfolding), you may get a crumpled mess that needs to be smoothed out (unfolding) to try to start the process over again (refolding), or you may just give up and feed it to the shredder for recycling (degradation). Some unfolded or misfolded conformations can aggregate and generate forms that are difficult to degrade, akin to a pile of sheets glued together, and cause cellular toxicity or death. In fact, defects in protein folding have been linked to a number of pathologies where such aggregates (amyloids) are observed, including neurodegenerative conditions such as Parkinson’s, Alzheimer’s and Huntington’s diseases, although what the toxic species are remains to be determined.”
Many of these concepts are covered in the Reviews and Progress articles that comprise a Nature Structural and Molecular Biology Focus on protein folding (free to read online), with an emphasis on recent developments in the field. Online features of the Focus include an annotated collection of ‘Classics’ —landmark papers that shaped and guided research. This compilation provides a historical perspective on how the field has progressed. The journal editors have also asked researchers about their views on where the field is going—the ‘big questions’ that still await answers and the technical developments that will make answering those questions possible; you can read these in ‘Looking ahead’. And you can browse a library of recent papers on protein folding published in the Nature journals.