Stability of Designed Proteins against Mutations

 
Thumbnail
View/Open
Author
Broglia, R. A.
Tiana, G.
Roman, H. E.
Vigezzi, E.
Shakhnovich, E.
Published Version
https://doi.org/10.1103/PhysRevLett.82.4727
Metadata
Show full item record
Citation
Broglia, R. A., G. Tiana, H. E. Roman, E. Vigezzi, and E. Shakhnovich. 1999. “Stability of Designed Proteins against Mutations.” Physical Review Letters 82 (23): 4727–30. https://doi.org/10.1103/physrevlett.82.4727.
Abstract
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 the "native" conformation. By a complete enumeration of the sequences obtained by introducing up to four point mutations and up to seven composition-conserving mutations (swapping of amino acids) in a 36mers chain and by running dynamic simulations on the mutated sequences, it is found that this number depends on the gap between the native conformation and the bulk of misfolded conformations, but not on the particular designed sequence, provided its associated energy gap is large. [S0031-9007(99)09339-4].
Terms of Use
This article is made available under the terms and conditions applicable to Other Posted Material, as set forth at http://nrs.harvard.edu/urn-3:HUL.InstRepos:dash.current.terms-of-use#LAA
Citable link to this page
http://nrs.harvard.edu/urn-3:HUL.InstRepos:41417277

Collections