A. G. Day

Step-wise mutation of barnase to binase. A procedure for engineering increased stability of proteins and an experimental analysis of the evolution of protein stability.

A. G. Day, L Serrano, A. Fersht, 1993, Journal of molecular biology.

Barnase has subsites that give rise to large rate enhancements.

A. Fersht, T. Brown, A. G. Day, 1992, Biochemistry.

Mutation of asparagine 111 of rubisco from Rhodospirillum rubrum alters the carboxylase/oxygenase specificity.

A. Fersht, P. Chène, A. G. Day, 1992, Journal of molecular biology.

Role of phenylalanine-327 in the closure of loop 6 of ribulosebisphosphate carboxylase/oxygenase from Rhodospirillum rubrum.

A. Fersht, P. Chène, A. G. Day, 1993, Biochemistry.

Role of isoleucine-164 at the active site of rubisco from Rhodospirillum rubrum.

A. Fersht, P. Chène, A. G. Day, 1997, Biochemical and biophysical research communications.

Refolding of barnase mutants and pro‐barnase in the presence and absence of GroEL.

A. Fersht, M. Bycroft, A. G. Day, 1993, The EMBO journal.

Order-by-disorder near criticality inXYpyrochlore magnets

A. G. Day, M. Gingras, B. Javanparast, 2015, 1506.05806.

Reaction of modified and unmodified tRNA(Tyr) substrates with tyrosyl-tRNA synthetase (Bacillus stearothermophilus).

A. Fersht, A. G. Day, J. Avis, 1993, Biochemistry.