D E Otzen

Folding of circular permutants with decreased contact order: general trend balanced by protein stability.

A. Finkelstein, A. V. Finkelstein, D. Otzen, 2001, Journal of molecular biology.

Analysis of protein-protein interactions by mutagenesis: direct versus indirect effects.

A. Fersht, D. Otzen, D E Otzen, 1999, Protein engineering.

Designed protein tetramer zipped together with a hydrophobic Alzheimer homology: a structural clue to amyloid assembly.

D. Otzen, M. Oliveberg, O. Kristensen, 2000, Proceedings of the National Academy of Sciences of the United States of America.

Single versus parallel pathways of protein folding and fractional formation of structure in the transition state.

A. Fersht, L. Itzhaki, D. Otzen, 1994, Proceedings of the National Academy of Sciences of the United States of America.

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.

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

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

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

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

Movement of the position of the transition state in protein folding.

A. Fersht, L. Itzhaki, D. Otzen, 1995, Biochemistry.

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.

Structure of the transition state for the folding/unfolding of the barley chymotrypsin inhibitor 2 and its implications for mechanisms of protein folding.

A. Fersht, L. Itzhaki, D. Otzen, 1994, Proceedings of the National Academy of Sciences of the United States of America.