Abstract
Protein Folding: Past and Future Fifty years ago the Nobel Prize in chemistry was awarded to Max Perutz and John Kendrew for determining the structure of globular proteins. Since first viewing their structure of myoglobin, scientists have sought to understand protein folding. Dill and MacCallum (p. 1042 ) review the progress that has been made on three central questions: What is the code that relates sequence to structure? How do proteins fold so fast? Can protein structure be computationally predicted? While we have come some way toward answering these questions, new questions have been gene rated. It is no longer useful to talk about “solving the protein-folding problem”—protein folding has grown into a field of research where the next 50 years promise to be as exciting as the last.
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Dates
Type | When |
---|---|
Created | 12 years, 9 months ago (Nov. 22, 2012, 2:24 p.m.) |
Deposited | 1 year, 7 months ago (Jan. 10, 2024, 9:52 a.m.) |
Indexed | 27 minutes ago (Aug. 25, 2025, 10:53 p.m.) |
Issued | 12 years, 9 months ago (Nov. 23, 2012) |
Published | 12 years, 9 months ago (Nov. 23, 2012) |
Published Print | 12 years, 9 months ago (Nov. 23, 2012) |
@article{Dill_2012, title={The Protein-Folding Problem, 50 Years On}, volume={338}, ISSN={1095-9203}, url={http://dx.doi.org/10.1126/science.1219021}, DOI={10.1126/science.1219021}, number={6110}, journal={Science}, publisher={American Association for the Advancement of Science (AAAS)}, author={Dill, Ken A. and MacCallum, Justin L.}, year={2012}, month=nov, pages={1042–1046} }