Carolyn M. Teschke

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.

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 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.