M Bycroft

Application of thermophilic enzymes in commercial biotransformation processes.

I N Taylor, R C Brown, M Bycroft, 2004, Biochemical Society transactions.

Stabilization of protein structure by interaction of alpha-helix dipole with a charged side chain.

M Bycroft, A. Fersht, M. Bycroft, 1988, Nature.

A comparison of the pH, urea, and temperature-denatured states of barnase by heteronuclear NMR: implications for the initiation of protein folding.

V L Arcus, M Bycroft, A. Fersht, 1995, Journal of molecular biology.

The UBX domain: a widespread ubiquitin-like module.

M Bycroft, M. Bycroft, M. Proctor, 2001, Journal of molecular biology.

Hot-spot mutants of p53 core domain evince characteristic local structural changes.

M Bycroft, A. Fersht, M. Bycroft, 1999, Proceedings of the National Academy of Sciences of the United States of America.

Aromatic-aromatic interactions and protein stability. Investigation by double-mutant cycles.

L Serrano, M Bycroft, A. Fersht, 1991, Journal of molecular biology.

Characterization of phosphate binding in the active site of barnase by site-directed mutagenesis and NMR.

M Bycroft, A. Fersht, M. Bycroft, 1991, Biochemistry.

The structure of a LysM domain from E. coli membrane-bound lytic murein transglycosylase D (MltD).

M Bycroft, A. Bateman, M. Bycroft, 2000, Journal of molecular biology.