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Published August 2006 | public
Journal Article

Simple electrostatic model improves designed protein sequences


Electrostatic interactions are important for both protein stability and function, including binding and catalysis. As protein design moves into these areas, an accurate description of electrostatic energy becomes necessary. Here, we show that a simple distance-dependent Coulombic function parameterized by a comparison to Poisson-Boltzmann calculations is able to capture some of these electrostatic interactions. Specifically, all three helix N-capping interactions in the engrailed homeodomain fold are recovered using the newly parameterized model. The stability of this designed protein is similar to a protein forced by sequence restriction to have beneficial electrostatic interactions.

Additional Information

© 2006 The Protein Society. Published by Cold Spring Harbor Laboratory Press. Received January 24, 2006; Final Revision May 12, 2006; Accepted May 15, 2006. Article first published online: 1 Jan. 2009. This work was supported by the Howard Hughes Medical Institute and the Ralph M. Parsons Foundation. E.S.Z. would like to thank the ARCS Foundation for funding.

Additional details

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