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. 1989 Apr;86(7):2152–2156. doi: 10.1073/pnas.86.7.2152

Identifying determinants of folding and activity for a protein of unknown structure.

J U Bowie 1, R T Sauer 1
PMCID: PMC286869  PMID: 2928323

Abstract

We have generated an extensive genetic map of functionally allowed and/or structurally allowed amino acid substitutions in Arc repressor, a DNA binding protein of unknown structure. Analysis of the allowed substitution patterns identifies residues that are likely to be involved in protein function and identifies side chains that play important structural roles, including residues likely to form the hydrophobic core. The identities of approximately one-third of the residues in Arc repressor are functionally important, about one-half are structurally important, and the remainder are unimportant for either structure or function. The patterns of obligatory hydrophobic positions permit strong predictions of secondary structure.

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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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