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Phosphorylation destabilizes α-helices

Nature Structural Biology volume 4, pages 112–114 (1997)Cite this article

Abstract

Phosphorylation of threonine destabilizes the leucine zipper of a bZIP protein by 4.6 kcal mol−1 dimer−1, which reduces DNA binding 100-fold. This decrease in stability reflects the low α-helix forming propensity of a phosphorylated threonine.

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Authors and Affiliations

  1. Laboratory of Biochemistry, National Cancer Institute, National Institutes of Health, Building 37, Room 4D06, Bethesda, Maryland, 20892, USA

    László Szilák, Jaideep Moitra, Dmitry Krylov & Charles Vinson

Authors
  1. László Szilák
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  2. Jaideep Moitra
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  3. Dmitry Krylov
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  4. Charles Vinson
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Correspondence to Charles Vinson.

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Szilák, L., Moitra, J., Krylov, D. et al. Phosphorylation destabilizes α-helices. Nat Struct Mol Biol 4, 112–114 (1997). https://doi.org/10.1038/nsb0297-112

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