Some of the principles underlying how amino-acid sequences determine the three-dimensional structures of proteins have been defined. This has enabled a successful approach to designing protein folds from scratch. See Article p.222
This is a preview of subscription content, access via your institution
Access options
Subscribe to this journal
Receive 51 print issues and online access
$199.00 per year
only $3.90 per issue
Buy this article
- Purchase on Springer Link
- Instant access to full article PDF
Prices may be subject to local taxes which are calculated during checkout
References
Koga, N. et al. Nature 491, 222–227 (2012).
Leopold, P. E., Montal, M. & Onuchic, J. N. Proc. Natl Acad. Sci. USA 89, 8721–8725 (1992).
Ramachandran, G. N., Ramakrishnan, C. & Sasisekharan, V. J. Mol. Biol. 7, 95–99 (1963).
Kuhlman, B. et al. Science 302, 1364–1368 (2003).
Röthlisberger, D. et al. Nature 453, 190–195 2008).
Korendovych, I. V. et al. Proc. Natl Acad. Sci. USA 108, 6823–6827 (2011).
Baker, D. Protein Sci. 19, 1817–1819 (2010).
Schreier, B., Stumpp, C., Wiesner, S. & Höcker, B. Proc. Natl Acad. Sci. USA 106, 18491–18496 (2009).
Sterner, R. & Höcker, B. Chem. Rev. 105, 4038–4055 (2005).
Author information
Authors and Affiliations
Corresponding author
Rights and permissions
About this article
Cite this article
Höcker, B. A toolbox for protein design. Nature 491, 204–205 (2012). https://doi.org/10.1038/491204a
Published:
Issue Date:
DOI: https://doi.org/10.1038/491204a
This article is cited by
-
Critical Role of a Loop at C-Terminal Domain on the Conformational Stability and Catalytic Efficiency of Chondroitinase ABC I
Molecular Biotechnology (2015)
-
Evolutionary relationship of two ancient protein superfolds
Nature Chemical Biology (2014)
