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Protein stability effects of a complete set of alanine substitutions in Arc repressor

Nature Structural Biology volume 1, pages 518–523 (1994)Cite this article

An Erratum to this article was published on 01 November 1994

Abstract

The equilibrium stabilities of a complete set of single alanine-substitution mutants of the Arc repressor of bacteriophage P22 have been determined by thermal and urea denaturation experiments. Only half the alanine substitutions cause significant changes in stability, with the most deleterious mutations affecting side chains in the hydrophobic core or in salt bridges and hydrogen bonds which are protected from solvent. The five mutations that are most destabilizing affect a cluster of core residues that seem to form a structural foundation for Arc.

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Author notes

  1. Marcos E. Milla

    Present address: Deptartment of Biochemistry, Duke University Medical Center, Durham, North Carolina, 27710, USA

Authors and Affiliations

  1. Department of Biology, Massachusetts Institute of Technology, Cambridge, Massachusetts, 02139, USA

    Marcos E. Milla, Bronwen M. Brown & Robert T. Sauer

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Milla, M., Brown, B. & Sauer, R. Protein stability effects of a complete set of alanine substitutions in Arc repressor. Nat Struct Mol Biol 1, 518–523 (1994). https://doi.org/10.1038/nsb0894-518

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