Phosphorylation destabilizes alpha-helices. (Q54571573)

1 June 2018

title

Phosphorylation destabilizes alpha-helices. (English)

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1 June 2018

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Szilák L

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1 June 2018

Moitra J

series ordinal

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1 June 2018

Krylov D

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1 June 2018

Vinson C

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1 June 2018

publication date

1 February 1997

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1 June 2018

Nature structural biology

published in

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1 June 2018

volume

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issue

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page(s)

112-114

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The regulation of transcription by phosphorylation

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Large differences in the helix propensities of alanine and glycine

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Determination of alpha-helix propensity within the context of a folded protein. Sites 44 and 131 in bacteriophage T4 lysozyme

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Cyclic AMP stimulates somatostatin gene transcription by phosphorylation of CREB at serine 133

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Evidence of changes in protease sensitivity and subunit exchange rate on DNA binding by C/EBP.

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Structure of a peptide inhibitor bound to the catalytic subunit of cyclic adenosine monophosphate-dependent protein kinase

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A CORRELATION BETWEEN AMINO ACID COMPOSITION AND PROTEIN STRUCTURE.

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A thermodynamic scale for the helix-forming tendencies of the commonly occurring amino acids

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Structural basis of amino acid alpha helix propensity

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Side-chain entropy opposes alpha-helix formation but rationalizes experimentally determined helix-forming propensities

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Alpha-helix stabilization by natural and unnatural amino acids with alkyl side chains

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The energetics of ion-pair and hydrogen-bonding interactions in a helical peptide

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Mechanism of specificity in the Fos-Jun oncoprotein heterodimer

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Dimerization specificity of the leucine zipper-containing bZIP motif on DNA binding: prediction and rational design

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Separation of phospho‐ and non‐phosphopeptides using reverse phase column chromatography

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31 March 2020

Identifiers

DOI

10.1038/NSB0297-112

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1 June 2018

Dimensions Publication ID

1022018582

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1 June 2018