J. Boisbouvier

This paper introduces a method to site-specifically incorporate isotopically labeled alanines into proteins for NMR studies, enabling structural analysis of large biomolecular assemblies and low-complexity regions.

The paper identifies a metastable excited state in the HSP90 ATP binding domain using solution NMR and mutagenesis, showing it transiently samples a closed state distant from the ground state.

This study shows how prefoldin inhibits IAPP fibril formation by binding to the N-terminal segment of IAPP on fibril surfaces and ends, reducing aggregate size and number.

The paper integrates NMR and cryo-EM to determine the atomic structure of a large enzyme complex, achieving high precision and accuracy beyond the limitations of each method individually.