Phosphorylation destabilizes α-helices

L. Szilak, J. Moitra, D. Krylov, C. Vinson

Research output: Contribution to journalArticle

72 Citations (Scopus)


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.

Original languageEnglish
Pages (from-to)112-114
Number of pages3
JournalNature Structural Biology
Issue number2
Publication statusPublished - Feb 20 1997

ASJC Scopus subject areas

  • Structural Biology
  • Biochemistry
  • Genetics

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