Designability and thermal stability of protein structures

Ned S. Wingreen, Hao Li, Chao Tang

Research output: Contribution to journalArticlepeer-review

31 Scopus citations


Only about 1000 qualitatively different protein folds are believed to exist in nature. Here, we review theoretical studies which suggest that some folds are intrinsically more designable than others, i.e. are lowest energy states of an unusually large number of sequences. The sequences associated with these folds are also found to be unusually thermally stable. The connection between highly designable structures and highly stable sequences is generally known as the 'designability principle'. The designability principle may help explain the small number of natural folds, and may also guide the design of new folds.

Original languageEnglish (US)
Pages (from-to)699-705
Number of pages7
Issue number2
StatePublished - Jan 15 2004

All Science Journal Classification (ASJC) codes

  • Organic Chemistry
  • Polymers and Plastics
  • Materials Chemistry


  • Lattice models
  • Off-lattice models
  • Protein folding


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