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. 1993 Aug 1;90(15):7195–7199. doi: 10.1073/pnas.90.15.7195

Engineering of stable and fast-folding sequences of model proteins.

E I Shakhnovich 1, A M Gutin 1
PMCID: PMC47103  PMID: 8346235

Abstract

The statistical mechanics of protein folding implies that the best-folding proteins are those that have the native conformation as a pronounced energy minimum. We show that this can be obtained by proper selection of protein sequences and suggest a simple practical way to find these sequences. The statistical mechanics of these proteins with optimized native structure is discussed. These concepts are tested with a simple lattice model of a protein with full enumeration of compact conformations. Selected sequences are shown to have a native state that is very stable and kinetically accessible.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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