Journal
JOURNAL OF MOLECULAR BIOLOGY
Volume 372, Issue 1, Pages 1-6Publisher
ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
DOI: 10.1016/j.jmb.2007.06.032
Keywords
computational protein design; NMR structure; protein stability; engrailed homeodomain; FASTER
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Computational protein design procedures were applied to the redesign of the entire sequence of a 51 amino acid residue protein, Drosophila melanogaster engrailed homeodomain. Various sequence optimization algorithms were compared and two resulting designed sequences were experimentally evaluated. The two sequences differ by 11 mutations and share 22% and 24% sequence identity with the wild-type protein. Both computationally designed proteins were considerably more stable than the than 99 degrees C. The solution structure was determined for one of the two sequences using multidimensional heteronuclear NMR spectroscopy, and the structure was found to closely match the original design template scaffold. (c) 2007 Elsevier Ltd. All rights reserved.
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