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. 1995 Aug 29;92(18):8438–8442. doi: 10.1073/pnas.92.18.8438

Conformation, energy, and folding ability of selected amino acid sequences.

M Sasai 1
PMCID: PMC41172  PMID: 7667308

Abstract

Evolutionary selection of sequences is studied with a knowledge-based Hamiltonian to find the design principle for folding to a model protein structure. With sequences selected by naive energy minimization, the model structure tends to be unstable and the folding ability is low. Sequences with high folding ability have only the low-lying energy minimum but also an energy landscape which is similar to that found for the native sequence over a wide region of the conformation space. Though there is a large fluctuation in foldable sequences, the hydrophobicity pattern and the glycine locations are preserved among them. Implications of the design principle for the molecular mechanism of folding are discussed.

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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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