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Article

Effect of mutations mimicking phosphorylation on the structure and properties of human 14-3-3zeta.

Archives of biochemistry and biophysics - 15 Sept 2008

Sluchanko Nikolai N, Chernik Ivan S, Seit-Nebi Alim S, Pivovarova Anastasia V, Levitsky Dmitrii I, Gusev Nikolai B

Abstract excerpt

Effect of mutations mimicking phosphorylation on the structure of human 14-3-3zeta protein was analyzed by different methods. Mutation S58E increased intrinsic Trp fluorescence and binding of bis-ANS to 14-3-3. At low protein concentration mutation S58E increased the probability of dissociation of dimeric 14-3-3 and its susceptibility to proteolysis. Mutation S184E slightly increased Stokes radius and thermal...

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Source

Identifiers

PMID: 18559254
DOI: 10.1016/j.abb.2008.05.020

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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