Daniel E. Otzen

The diversity of FtsY-lipid interactions.

J. Enghild, I. Thøgersen, M. E. Reinau, 2010, Biopolymers.

Folding of circular and permuted chymotrypsin inhibitor 2: retention of the folding nucleus.

A. Fersht, D. Otzen, D E Otzen, 1998, Biochemistry.

Structure of the transition state for folding of a protein derived from experiment and simulation.

A. Fersht, A. Li, V. Daggett, 1996, Journal of molecular biology.

Electrostatics in the active site of an alpha-amylase.

T. Borchert, J. Nielsen, D. Otzen, 1999, European journal of biochemistry.

Salt-induced detour through compact regions of the protein folding landscape.

D. Otzen, M. Oliveberg, Daniel E. Otzen, 1999, Proceedings of the National Academy of Sciences of the United States of America.

Conformational pathway of the polypeptide chain of chymotrypsin inhibitor-2 growing from its N terminus in vitro. Parallels with the protein folding pathway.

A. Fersht, D. Otzen, J. Neira, 1995, Journal of molecular biology.

Structural changes in the transition state of protein folding: alternative interpretations of curved chevron plots.

M. Proctor, D. Otzen, M. Oliveberg, 1999, Biochemistry.