BIOPHYSICS. For the article “Conversion of monomeric protein L to an obligate dimer by computational protein design,” by Brian Kuhlman, Jason W. O'Neill, David E. Kim, Kam Y. J. Zhang, and David Baker, which appeared in number 19, September 11, 2001, of Proc. Natl. Acad. Sci. USA (98, 10687–10691; First Published August 28, 2001; 10.1073/pnas.181354398), the authors note the following. In the Introduction and Discussion of our paper, we failed to reference a recent article by Rousseau et al. (1), which demonstrated that single point mutations can significantly perturb the equilibrium between monomeric and domain-swapped dimeric p13suc1. Rational methods were used to redesign p13suc1 from a fully monomeric protein (dissociation constant of ≈900 mM) to a fully dimeric protein (dissociation constant of ≈100 nM). 1. Rousseau, F., Schymkowitz, J. W. H., Wilkinson, H. R. & Itzhaki, L. S. (2001) Proc. Natl. Acad. Sci. USA 98, 5596–5601.
. 2002 May 21;99(11):7809. doi: 10.1073/pnas.112147399
Correction
Issue date 2002 May 28.
Copyright © 2002, The National Academy of Sciences
PMCID: PMC124426
This corrects the article "Conversion of monomeric protein L to an obligate dimer by computational protein design" in volume 98 on page 10687.
This corrects the article "Three-dimensional domain swapping in p13suc1 occurs in the
unfolded state and is controlled by conserved proline residues" in volume 98 on page 5596.