A R Fersht

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Strain in the folding nucleus of chymotrypsin inhibitor 2.

A. Fersht, L. Itzhaki, A. Ladurner, 1997, Folding & design.

Mutational analysis of the N-capping box of the alpha-helix of chymotrypsin inhibitor 2.

A. Fersht, N. Elmasry, A R Fersht, 1994, Protein engineering.

Search for nucleation sites in smaller fragments of chymotrypsin inhibitor 2.

A. Fersht, L. Itzhaki, J. Neira, 1995, Journal of molecular biology.

The folding of an enzyme. IV. Structure of an intermediate in the refolding of barnase analysed by a protein engineering procedure.

L Serrano, A. Fersht, L. Serrano, 1992, Journal of molecular biology.

Energetics of protein-protein interactions: analysis of the barnase-barstar interface by single mutations and double mutant cycles.

G Schreiber, A. Fersht, G. Schreiber, 1995, Journal of molecular biology.

Mechanism of rescue of common p53 cancer mutations by second‐site suppressor mutations

A. Fersht, B. DeDecker, P. Nikolova, 2000, The EMBO journal.

Importance of two buried salt bridges in the stability and folding pathway of barnase.

A. Fersht, S. Vuilleumier, A. Tissot, 1996, Biochemistry.

A search for single substitutions that eliminate enzymatic function in a bacterial ribonuclease.

A. Fersht, D. Axe, A R Fersht, 1998, Biochemistry.

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

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

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.

Mapping the structures of transition states and intermediates in folding: delineation of pathways at high resolution.

A. Fersht, A R Fersht, 1995, Philosophical transactions of the Royal Society of London. Series B, Biological sciences.

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

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

Thermodynamic stability and folding of GroEL minichaperones.

A. Fersht, S. Harding, R. Zahn, 1998, Journal of molecular biology.

Contribution of a proline residue and a salt bridge to the stability of a type I reverse turn in chymotrypsin inhibitor-2.

A. Fersht, A R Fersht, G de Prat Gay, 1994, Protein engineering.

Active barnase variants with completely random hydrophobic cores.

A. Fersht, D. Axe, A R Fersht, 1996, Proceedings of the National Academy of Sciences of the United States of America.

Strategy for analysing the co-operativity of intramolecular interactions in peptides and proteins.

A. Fersht, A. Horovitz, A R Fersht, 1990, Journal of molecular biology.

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.

Initiation sites of protein folding by NMR analysis.

A. Fersht, S. Freund, K. B. Wong, 1996, Proceedings of the National Academy of Sciences of the United States of America.

Interaction of barnase with its polypeptide inhibitor barstar studied by protein engineering.

G Schreiber, A. Fersht, G. Schreiber, 1993, Biochemistry.

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.

Energetics of complementary side-chain packing in a protein hydrophobic core.

A. Fersht, J. Kellis, K. Nyberg, 1989, Biochemistry.

Effect of cavity-creating mutations in the hydrophobic core of chymotrypsin inhibitor 2.

A. Fersht, C. M. Johnson, S. Jackson, 1993, Biochemistry.

Electrostatic enhancement of diffusion-controlled protein-protein association: comparison of theory and experiment on barnase and barstar.

G Schreiber, A. Fersht, G. Schreiber, 1998, Journal of molecular biology.

Thermodynamic study of the acid denaturation of barnase and its dependence on ionic strength: evidence for residual electrostatic interactions in the acid/thermally denatured state.

A. Fersht, S. Vuilleumier, M. Oliveberg, 1994, Biochemistry.

Conversion of two-state to multi-state folding kinetics on fusion of two protein foldons.

A. Fersht, K. Inaba, N. Kobayashi, 2000, Journal of molecular biology.

Variants of subtilisin BPN' with altered specificity profiles.

A. Fersht, J. Eder, A R Fersht, 1994, Biochemistry.

Folding of chymotrypsin inhibitor 2. 1. Evidence for a two-state transition.

A. Fersht, S. Jackson, A R Fersht, 1991, Biochemistry.

Characterization of residual structure in the thermally denatured state of barnase by simulation and experiment: description of the folding pathway.

C. J. Bond, A. Fersht, V. Daggett, 1997, Proceedings of the National Academy of Sciences of the United States of America.

Submillisecond events in protein folding.

A. Fersht, R. Golbik, A R Fersht, 1995, Proceedings of the National Academy of Sciences of the United States of America.

Folding of a nascent polypeptide chain in vitro: cooperative formation of structure in a protein module.

A. Fersht, L. Itzhaki, J. Neira, 1995, 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.

Transition-state structure as a unifying basis in protein-folding mechanisms: contact order, chain topology, stability, and the extended nucleus mechanism.

A. Fersht, A R Fersht, 2000, Proceedings of the National Academy of Sciences of the United States of America.

Use of binding energy in catalysis analyzed by mutagenesis of the tyrosyl-tRNA synthetase.

A. Fersht, T. Wells, A R Fersht, 1986, Biochemistry.

Mutually compensatory mutations during evolution of the tetramerization domain of tumor suppressor p53 lead to impaired hetero-oligomerization.

A. Fersht, M. G. Mateu, A R Fersht, 1999, Proceedings of the National Academy of Sciences of the United States of America.

Retraction. Directed evolution of new catalytic activity using the alpha/beta-barrel scaffold.

J M Blackburn, A R Fersht, M M Altamirano, 2002, Nature.

Kinetic characterization of the recombinant ribonuclease from Bacillus amyloliquefaciens (barnase) and investigation of key residues in catalysis by site-directed mutagenesis.

A. Fersht, K. Nyberg, D. Mossakowska, 1989, Biochemistry.

Exploring the energy surface of protein folding by structure-reactivity relationships and engineered proteins: observation of Hammond behavior for the gross structure of the transition state and anti-Hammond behavior for structural elements for unfolding/folding of barnase.

A. Fersht, J. Matthews, A R Fersht, 1995, Biochemistry.

Perturbed pKA-values in the denatured states of proteins.

A. Fersht, B. Davis, M. Oliveberg, 1995, Journal of molecular biology.

The folding of an enzyme. II. Substructure of barnase and the contribution of different interactions to protein stability.

L Serrano, A. Fersht, L. Serrano, 1992, Journal of molecular biology.

pKA values of carboxyl groups in the native and denatured states of barnase: the pKA values of the denatured state are on average 0.4 units lower than those of model compounds.

V L Arcus, A. Fersht, V. Arcus, 1995, Biochemistry.

Structure of the hydrophobic core in the transition state for folding of chymotrypsin inhibitor 2: a critical test of the protein engineering method of analysis.

A. Fersht, S. Jackson, N. Elmasry, 1993, Biochemistry.

Synergy between simulation and experiment in describing the energy landscape of protein folding.

A. Fersht, V. Daggett, L. Itzhaki, 1998, Proceedings of the National Academy of Sciences of the United States of America.

Dissection of the structure and activity of the tyrosyl-tRNA synthetase by site-directed mutagenesis.

A. Fersht, A R Fersht, 1987, Biochemistry.

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.

Stabilization of GroEL minichaperones by core and surface mutations.

A. Fersht, A. Buckle, Q. Wang, 2000, Journal of molecular biology.

Design of highly stable functional GroEL minichaperones

A. Fersht, A. Buckle, A R Fersht, 1999, Protein science : a publication of the Protein Society.

Crystal structural analysis of mutations in the hydrophobic cores of barnase.

A. Fersht, K. Henrick, A. Buckle, 1994, Journal of molecular biology.

Folding of barnase in parts.

A. Fersht, J. Sancho, A. Kippen, 1994, Biochemistry.

Contribution of buried hydrogen bonds to protein stability. The crystal structures of two barnase mutants.

A. Fersht, K. Henrick, A R Fersht, 1993, Journal of molecular biology.

The folding of an enzyme. III. Structure of the transition state for unfolding of barnase analysed by a protein engineering procedure.

L Serrano, A. Fersht, L. Serrano, 1992, Journal of molecular biology.

Semirational design of active tumor suppressor p53 DNA binding domain with enhanced stability.

A. Fersht, D. Lane, P. Nikolova, 1998, Proceedings of the National Academy of Sciences of the United States of America.

Effect of active site residues in barnase on activity and stability.

L Serrano, A. Fersht, L. Serrano, 1992, Journal of molecular biology.

Protein folding and stability: the pathway of folding of barnase

A. Fersht, A R Fersht, 1993 .

Folding intermediates of wild-type and mutants of barnase. II. Correlation of changes in equilibrium amide exchange kinetics with the population of the folding intermediate.

J Clarke, A R Fersht, C M Johnson, 1998, Journal of molecular biology.

Protein folding and unfolding in microseconds to nanoseconds by experiment and simulation.

A. Fersht, V. Daggett, C. M. Johnson, 2000, Proceedings of the National Academy of Sciences of the United States of America.

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

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

Glutamine, alanine or glycine repeats inserted into the loop of a protein have minimal effects on stability and folding rates.

A. Fersht, A. Ladurner, A G Ladurner, 1997, Journal of molecular biology.

Thermodynamic stability of wild-type and mutant p53 core domain.

A. Fersht, B. DeDecker, M. Proctor, 1997, Proceedings of the National Academy of Sciences of the United States of America.

Characterizing transition states in protein folding: an essential step in the puzzle.

A. Fersht, A R Fersht, 1995, Current opinion in structural biology.

Directed evolution of new catalytic activity using the alpha/beta-barrel scaffold.

J M Blackburn, A R Fersht, M M Altamirano, 2000, Nature.

Pathway of protein folding.

L Serrano, A. Fersht, L. Serrano, 1992, Faraday discussions.

Stability and function: two constraints in the evolution of barstar and other proteins.

G Schreiber, A. Fersht, A. Buckle, 1994, Structure.

Folding of subtilisin BPN': characterization of a folding intermediate.

A. Fersht, J. Eder, A R Fersht, 1993, Biochemistry.

Alpha-helix stability in proteins. I. Empirical correlations concerning substitution of side-chains at the N and C-caps and the replacement of alanine by glycine or serine at solvent-exposed surfaces.

L Serrano, A. Fersht, L. Serrano, 1992, Journal of molecular biology.

Enzyme hyperspecificity. Rejection of threonine by the valyl-tRNA synthetase by misacylation and hydrolytic editing.

A. Fersht, A R Fersht, M. Kaethner, 1976, Biochemistry.

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

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

NMR analysis of the binding of a rhodanese peptide to a minichaperone in solution.

A. Fersht, S. Freund, N. Kobayashi, 1999, Journal of molecular biology.

Analysis of the role of the KMSKS loop in the catalytic mechanism of the tyrosyl-tRNA synthetase using multimutant cycles.

A. Fersht, A R Fersht, E A First, 1995, Biochemistry.

Kinetic significance of GroEL14.(GroES7)2 complexes in molecular chaperone activity.

A. Fersht, F. Corrales, A R Fersht, 1996, Folding & design.

Electrostatic effects on modification of charged groups in the active site cleft of subtilisin by protein engineering.

A. Fersht, P. Thomas, A. Russell, 1987, Journal of molecular biology.

Capping and alpha-helix stability.

L Serrano, A. Fersht, L. Serrano, 1989, Nature.

Exploring the folding funnel of a polypeptide chain by biophysical studies on protein fragments.

A. Fersht, J. Neira, A R Fersht, 1999, Journal of molecular biology.

The folding of an enzyme. VI. The folding pathway of barnase: comparison with theoretical models.

L Serrano, A. Fersht, L. Serrano, 1992, Journal of molecular biology.

Thermodynamics of the interaction of barnase and barstar: changes in free energy versus changes in enthalpy on mutation.

G Schreiber, A. Fersht, G. Schreiber, 1997, Journal of molecular biology.

Histidine-aromatic interactions in barnase. Elevation of histidine pKa and contribution to protein stability.

A. Fersht, J. Sancho, R. Loewenthal, 1992, Journal of molecular biology.

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.

Catalysis, binding and enzyme-substrate complementarity

A. Fersht, A R Fersht, 1974, Proceedings of the Royal Society of London. Series B. Biological Sciences.

The folding pathway of a protein at high resolution from microseconds to seconds.

G Schreiber, A. Fersht, G. Schreiber, 1997, Proceedings of the National Academy of Sciences of the United States of America.

The role of Glu73 of barnase in catalysis and the binding of barstar.

G Schreiber, A. Fersht, G. Schreiber, 1997, Journal of molecular biology.

Structural response to mutation at a protein-protein interface.

A. Fersht, A. Buckle, C. Vaughan, 1998, Journal of molecular biology.

An evaluation of the use of hydrogen exchange at equilibrium to probe intermediates on the protein folding pathway.

J Clarke, A R Fersht, 1996, Folding & design.

Editing mechanisms in protein synthesis. Rejection of valine by the isoleucyl-tRNA synthetase.

A. Fersht, A R Fersht, 1977, Biochemistry.

Subsite binding in an RNase: structure of a barnase-tetranucleotide complex at 1.76-A resolution.

A. Fersht, A. Buckle, A R Fersht, 1994, Biochemistry.

Structure-activity relationships in engineered proteins: analysis of use of binding energy by linear free energy relationships.

R J Leatherbarrow, A. Fersht, R. Leatherbarrow, 1987, Biochemistry.

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.