The coming of age of de novo protein design

Po-Ssu Huang, Scott E. Boyken and David Baker ()
Additional contact information
Po-Ssu Huang: University of Washington
Scott E. Boyken: University of Washington
David Baker: University of Washington

Nature, 2016, vol. 537, issue 7620, 320-327

Abstract: Abstract There are 20200 possible amino-acid sequences for a 200-residue protein, of which the natural evolutionary process has sampled only an infinitesimal subset. De novo protein design explores the full sequence space, guided by the physical principles that underlie protein folding. Computational methodology has advanced to the point that a wide range of structures can be designed from scratch with atomic-level accuracy. Almost all protein engineering so far has involved the modification of naturally occurring proteins; it should now be possible to design new functional proteins from the ground up to tackle current challenges in biomedicine and nanotechnology.

Date: 2016
References: Add references at CitEc
Citations: View citations in EconPapers (22)

Downloads: (external link)
https://www.nature.com/articles/nature19946 Abstract (text/html)
Access to the full text of the articles in this series is restricted.

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:nature:v:537:y:2016:i:7620:d:10.1038_nature19946

Ordering information: This journal article can be ordered from
https://www.nature.com/

DOI: 10.1038/nature19946

Access Statistics for this article

Nature is currently edited by Magdalena Skipper

More articles in Nature from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().