Characterizing transition states in protein folding: an essential step in the puzzle
AR Fersht
– Curr Opin Struct Biol
(1995)
5,
ASSOCIATION OF PROTEIN-FRAGMENTS THROUGH A 2ND-ORDER FOLDING REACTION - STRUCTURE OF THE ISOLATED FRAGMENTS AND EARLY EVENTS OF PROTEIN-FOLDING
GD GAV, J RUIZSANZ, B DAVIS, AR FERSHT
– PROTEIN ENGINEERING
(1995)
8,
Folding & Design: introduction to a new journal
AR Fersht, FE Cohen
– Folding & design
(1995)
1,
THE STRUCTURE OF THE TRANSITION-STATE FOR THE ASSOCIATION OF 2 FRAGMENTS OF THE BARLEY CHYMOTRYPSIN INHIBITOR-2 TO GENERATE NATIVE-LIKE PROTEIN - IMPLICATIONS FOR MECHANISMS OF PROTEIN-FOLDING
G de Prat Gay, J Ruiz-Sanz, B Davis, AR Fersht
– Proceedings of the National Academy of Sciences of the United States of America
(1994)
91,
STRUCTURE OF THE TRANSITION-STATE FOR THE FOLDING/UNFOLDING OF THE BARLEY CHYMOTRYPSIN INHIBITOR-2 AND ITS IMPLICATIONS FOR MECHANISMS OF PROTEIN-FOLDING
DE Otzen, LS Itzhaki, NF elMasry, SE Jackson, AR Fersht
– Proceedings of the National Academy of Sciences
(1994)
91,
Single versus parallel pathways of protein folding and fractional formation of structure in the transition state.
AR Fersht, LS Itzhaki, NF elMasry, JM Matthews, DE Otzen
– Proc Natl Acad Sci U S A
(1994)
91,
Stability and function: two constraints in the evolution of barstar and other proteins
G Schreiber, AM Buckle, AR Fersht
– Structure (London, England : 1993)
(1994)
2,
Toward solving the folding pathway of barnase: the complete backbone 13C, 15N, and 1H NMR assignments of its pH-denatured state.
VL Arcus, S Vuilleumier, SM Freund, M Bycroft, AR Fersht
– Proceedings of the National Academy of Sciences of the United States of America
(1994)
91,
Extrapolation to water of kinetic and equilibrium data for the unfolding of barnase in urea solutions
A Matouschek, JM Matthews, CM Johnson, AR Fersht
– Protein Eng
(1994)
7,
Mutational analysis of the N-capping box of the α-helix of chymotrypsin inhibitor 2
NF elMasry, AR Fersht
– Protein Eng
(1994)
7,
