Optimization of rates of protein folding: the nucleation-condensation mechanism and its implications.
AR Fersht
– Proc Natl Acad Sci U S A
(1995)
92,
Submillisecond events in protein folding.
B Nölting, R Golbik, AR Fersht
– Proceedings of the National Academy of Sciences of the United States of America
(1995)
92,
DISULFIDE MUTANTS OF BARNASE .1. CHANGES IN STABILITY AND STRUCTURE ASSESSED BY BIOPHYSICAL METHODS AND X-RAY CRYSTALLOGRAPHY
J Clarke, K Henrick, AR Fersht
– J Mol Biol
(1995)
253,
DISULFIDE MUTANTS OF BARNASE .2. CHANGES IN STRUCTURE AND LOCAL STABILITY IDENTIFIED BY HYDROGEN-EXCHANGE
J Clarke, AM Hounslow, AR Fersht
– J Mol Biol
(1995)
253,
Negative activation enthalpies in the kinetics of protein folding.
M Oliveberg, YJ Tan, AR Fersht
– Proceedings of the National Academy of Sciences
(1995)
92,
The folding of GroEL-bound barnase as a model for chaperonin-mediated protein folding.
FJ Corrales, AR Fersht
– Proceedings of the National Academy of Sciences of the United States of America
(1995)
92,
Energetics of protein-protein interactions: Analysis ofthe Barnase-Barstar interface by single mutations and double mutant cycles
G Schreiber, AR Fersht
– Journal of Molecular Biology
(1995)
248,
Folding of a nascent polypeptide chain in vitro: cooperative formation of structure in a protein module.
G De Prat Gay, J Ruiz-Sanz, JL Neira, LS Itzhaki, AR Fersht
– Proceedings of the National Academy of Sciences
(1995)
92,
TOWARD SOLVING THE FOLDING PATHWAY OF BARNASE - THE BACKBONE C-13, N-15 AND H-1-NMR ASSIGNMENTS OF ITS PH-DENATURED AND UREA-DENATURED STATES
VL ARCUS, S VUILLEUMIER, SMV FREUND, M BYCROFT, AR FERSHT
– JOURNAL OF CELLULAR BIOCHEMISTRY
(1995)
Crystallographic analysis of Phe→Leu substitution in the hydrophobic core of barnase
YW Chen, AR Fersht, K Henrick
– Acta Crystallographica Section D, Structural Biology
(1995)
51,
