Publications by Nicolas Kellershohn

Publications by authors named "Nicolas Kellershohn"

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Kinetic analysis of R67 dihydrofolate reductase folding: from the unfolded monomer to the native tetramer.

Christophe Bodenreider Nicolas Kellershohn Michel E Goldberg Annick Méjean

Biochemistry

December 2002

R67 dihydrofolate reductase (DHFR) is a homotetrameric enzyme. Its subunit has a core structure consisting of five antiparallel beta-strands that form a compact beta-barrel. Our interest was to describe the molecular mechanism of the complete folding pathway of this beta-sheet protein, focusing on how the oligomerization steps are coordinated with the formation of secondary and tertiary structures all along the folding process.

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- Nicolas Kellershohn's research primarily focuses on the kinetic analysis and molecular mechanisms of protein folding, particularly in relation to oligomerization and structural formation.
- One of his notable studies investigates the folding pathway of R67 dihydrofolate reductase, emphasizing the intricate coordination between oligomerization and the development of secondary and tertiary structures during the folding process.
- Kellershohn's work contributes significant insights into the understanding of beta-sheet protein dynamics, which is critical for elucidating folding mechanisms in homotetrameric enzymes.

Publications by authors named "Nicolas Kellershohn"

Kinetic analysis of R67 dihydrofolate reductase folding: from the unfolded monomer to the native tetramer.

Synopsis of recent research by authors named "Nicolas Kellershohn"