Designability and thermal stability of protein structures

Abstract 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.

• Publication year

  2003

• Venue

  Polymer

• Publication date

  2003-03-28

• Fields of study

  Biology, Physics, Chemistry

• Identifiers
  DOI 10.1016/J.POLYMER.2003.10.062arXiv cond-mat/0303600
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar

• No claims are published for this paper.

• No concepts are published for this paper.

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