Phosphorylation destabilizes α-helices

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

Research output: Contribution to journalArticle

70 Citations (Scopus)

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.

Original languageEnglish
Pages (from-to)112-114
Number of pages3
JournalNature Structural Biology
Volume4
Issue number2
DOIs
Publication statusPublished - 1997

Fingerprint

Phosphorylation
Threonine
Basic-Leucine Zipper Transcription Factors
Leucine Zippers
Dimers
DNA

ASJC Scopus subject areas

  • Biochemistry
  • Structural Biology
  • Genetics

Cite this

Phosphorylation destabilizes α-helices. / Szilák, L.; Moitra, J.; Krylov, D.; Vinson, C.

In: Nature Structural Biology, Vol. 4, No. 2, 1997, p. 112-114.

Research output: Contribution to journalArticle

Szilák, L, Moitra, J, Krylov, D & Vinson, C 1997, 'Phosphorylation destabilizes α-helices', Nature Structural Biology, vol. 4, no. 2, pp. 112-114. https://doi.org/10.1038/nsb0297-112
Szilák, L. ; Moitra, J. ; Krylov, D. ; Vinson, C. / Phosphorylation destabilizes α-helices. In: Nature Structural Biology. 1997 ; Vol. 4, No. 2. pp. 112-114.
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