Melinda Roy

TL;DR: In mice xenografted with human tumor cells secreting matrix metalloproteinases 2 and 9, ACPPs bearing a far-red-fluorescent cargo show in vivo contrast ratios of 2-3 and a 3.1-fold increase in standard uptake value for tumors relative to contralateral normal tissue or control peptides with scrambled linkers.

TL;DR: The biophysical properties of mitoNEET suggest that it may participate in a redox-sensitive signaling and/or in Fe–S cluster transfer and the NEET fold, a unique dimeric structure that constitutes a new fold to not only the reported Fe-S protein structures but also to all known proteins.

TL;DR: The solution structure of the type II PKA R-subunit fragment RIIα(1–44) is reported, which encompasses both the AKAP-binding and dimerization interfaces and incorporates an X-type four-helix bundleDimerization motif with an extended hydrophobic face that is necessary for high-affinity AKAP binding.

TL;DR: The structures of two D/D‐AKAP peptide complexes obtained by solution NMR methods reveal conserved hydrophobic interaction surfaces on the helical AKAP peptides and the PKA R subunit, which are responsible for mediating the high affinity association in the complexes.

TL;DR: The folding of the β-sheet protein, interleukin-1β, was examined using pulse-labelling hydrogen exchange and electrospray ionization mass spectrometric analysis, as well as stopped-flow circular dichroism and fluorescence spectroscopies to provide kinetic evidence that formation of the native state of interleukaemia proceeds through an obligatory intermediate.