There has not been added a translated version of this content. You can either try searching or go to the "area" home page to see if you can find the information there

Biorecognition on the cover of FEBS Letters

After getting an article accepted in FEBS Letters, the authors sent a cover art suggestion to the journal. The image was accepted and is featured on the cover of FEBS Lett., Volume 585, Issue 8.

The interaction of 14-3-3 gamma with phospholipid membranes was studied using...
The interaction of 14-3-3 gamma with phospholipid membranes was studied using intrinsic tryptophan fluorescence
Jarl Underhaug and Helene Bustad Johannessen

Human 14-3-3 proteins contain two conserved tryptophan residues in each monomer, Trp60 and Trp233 in isoform γ. 14-3-3γ binds to negatively charged membranes and here we show that membrane binding can be monitored by steady-state intrinsic fluorescence spectroscopy. Measurements with W60F and W233F 14-3-3γ mutants revealed that Trp60 is the major contributor to the emission fluorescence, whereas the fluorescence of Trp233, which π-stacks with Tyr184, is quenched. The fluorescence is reduced and red-shifted upon specific binding of a phosphate ligand, and further red-shifted upon binding of 14-3-3γ to the membrane, compatible with solvent exposure of Trp60. Moreover, our results support that membrane binding involves the non-conserved, convex area of 14-3-3γ, and that Trp residues do not intercalate in the bilayer.

Read more in FEBS Letters