Andrei T. Alexandrescu

This paper uses high-pH NMR to identify hydrogen bonds and foldons in proteins, achieving higher accuracy than traditional methods.

This paper determines the solution structure of the CH-domain zinc finger from Makorin-3, revealing its metal-binding properties and potential role in protein interactions.

This paper characterizes abaecin-2, a hymenopteran HDP with copper-binding properties that can inhibit or protect bacteria depending on context.

The paper investigates the zinc-induced folding and solution structure of the ZC4H2 zinc finger, showing it folds around zinc with picomolar affinity and has a novel structural motif.

This paper studies the trimerization of the phage L decoration protein, showing that capsid templating accelerates its folding and that the C-terminal spike is essential for capsid binding.

The paper determines the solution structure of the Z0 domain of BCL11A and identifies sequence patterns distinguishing DNA-binding from non-binding zinc-fingers.

This study determines the structure of bacteriophage P22 scaffolding protein within its procapsid using magic-angle spinning NMR, revealing a trimer of dimers with both helical and disordered regions.

This study uses in-organello NMR to analyze how cardiolipin defects affect mitochondrial metabolism in yeast, showing altered metabolite kinetics and TCA cycle flux.

The paper shows that a previously thought non-functional zinc finger domain from ZNF711 can fold with three metal ligands and is catalytically active.

The paper uses NMR to show that the degenerate ZNF domain of ZNF750 binds Zn2+ with high affinity and forms a structured ββ fold, challenging the assumption that degenerate ZNFs are disordered.

This paper uses NMR to identify mobile segments of the phage P22 scaffolding protein in solution and within a procapsid complex, revealing the N-terminus remains disordered and negatively charged when bound.