Stability of Designed Proteins Against Mutations

Details Stability of Designed Proteins Against Mutations Stability of Designed Proteins Against Mutations

1998-09-30

arxiv.org/abs/cond-mat/9809410v1

Physics

Condensed Matter

Soft Condensed Matter

Scientific paper

10.1103/PhysRevLett.82.4727

The stability of model proteins with designed sequences is assessed in terms of the number of sequences (obtained from the designed sequence through mutations), which fold into 5the ``native'' conformation. By a complete enumeration of the total number of sequences obtained by introducing up to 4 point mutations and up to 7 composition--conserving mutations (swapping of amino acids) in a 36mers chain, it is found that there are $10^8-10^9$ sequences which in the folding process target onto the ``native'' conformation. Consequently, proteins with designed sequences display a remarkable degree of stability and, to a large extent, of designability.

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