Phosphorylation destabilizes α-helices
- 1 February 1997
- journal article
- Published by Springer Nature in Nature Structural & Molecular Biology
- Vol. 4 (2) , 112-114
- https://doi.org/10.1038/nsb0297-112
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 alpha-helix forming propensity of a phosphorylated threonine.Keywords
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