Phosphorylation destabilizes alpha-helices.
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.
Szilák
L
L
Moitra
J
J
Krylov
D
D
Vinson
C
C
D000595:Amino Acid Sequence; D050976:Basic-Leucine Zipper Transcription Factors; D001665:Binding Sites; D002151:Calorimetry; D002942:Circular Dichroism; D003001:Cloning, Molecular; D004268:DNA-Binding Proteins / Q000737:chemistry* / Q000378:metabolism; D019281:Dimerization; D004355:Drug Stability; D004926:Escherichia coli; D051790:G-Box Binding Factors; D016350:Leucine Zippers; D008961:Models, Structural; D008969:Molecular Sequence Data; D010766:Phosphorylation; D010769:Phosphothreonine; D011489:Protein Denaturation; D017433:Protein Structure, Secondary; D011994:Recombinant Proteins / Q000737:chemistry / Q000378:metabolism; D013912:Threonine; D014157:Transcription Factors
D050976:Basic-Leucine Zipper Transcription Factors; D004268:DNA-Binding Proteins; D051790:G-Box Binding Factors; D011994:Recombinant Proteins; D014157:Transcription Factors; D010769:Phosphothreonine; D013912:Threonine