Abstract
Nature uses about one thousand folds to make proteins. Has nature exhausted all possibilities? What are the physical constraints for a stable fold? Can we find new folds and design sequences to adopt the new folds? Recent theoretical progress on the understanding of the designability of protein structures sheds light on these questions. The ability to discover new folds and to synthesize proteins with new folds will find many applications in the pharmaceutical industry. At NECI we have developed efficient methods to screen for new folds, and computational efforts are tightly coupled with experimental approaches.
Original language | English (US) |
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Pages (from-to) | 242-245 |
Number of pages | 4 |
Journal | NEC Research and Development |
Volume | 43 |
Issue number | 4 |
State | Published - Oct 2002 |
All Science Journal Classification (ASJC) codes
- Electrical and Electronic Engineering
Keywords
- De novo design
- Designability
- Protein folds