We found a match
Your institution may have access to this item. Find your institution then sign in to continue.
- Title
De novo protein design: fully automated sequence selection.
- Authors
Dahiyat, B I; Mayo, S L
- Abstract
The first fully automated design and experimental validation of a novel sequence for an entire protein is described. A computational design algorithm based on physical chemical potential functions and stereochemical constraints was used to screen a combinatorial library of 1.9 x 10(27) possible amino acid sequences for compatibility with the design target, a betabetaalpha protein motif based on the polypeptide backbone structure of a zinc finger domain. A BLAST search shows that the designed sequence, full sequence design 1 (FSD-1), has very low identity to any known protein sequence. The solution structure of FSD-1 was solved by nuclear magnetic resonance spectroscopy and indicates that FSD-1 forms a compact well-ordered structure, which is in excellent agreement with the design target structure. This result demonstrates that computational methods can perform the immense combinatorial search required for protein design, and it suggests that an unbiased and quantitative algorithm can be used in various structural contexts.
- Publication
Science (New York, N.Y.), 1997, Vol 278, Issue 5335, p82
- ISSN
0036-8075
- Publication type
Journal Article
- DOI
10.1126/science.278.5335.82