Computational design of water-soluble α-helical barrels

Author:

Thomson Andrew R.1,Wood Christopher W.12,Burton Antony J.1,Bartlett Gail J.1,Sessions Richard B.2,Brady R. Leo2,Woolfson Derek N.12

Affiliation:

1. School of Chemistry, University of Bristol, Cantock’s Close, Bristol, BS8 1TS, UK.

2. School of Biochemistry, University of Bristol, Medical Sciences Building, University Walk, Bristol, BS8 1TD, UK.

Abstract

Building with alphahelical coiled coils Understanding how proteins fold into well-defined three-dimensional structures has been a longstanding challenge. Increased understanding has led to increased success at designing proteins that mimic existing protein folds. This raises the possibility of custom design of proteins with structures not seen in nature. Thomson et al. describe the design of channelcontaining α-helical barrels, and Huang et al. designed hyperstable helical bundles. Both groups used rational and computational design to make new protein structures based on α-helical coiled coils but took different routes to reach different target structures. Science , this issue p. 485 , p. 481

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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