Surface electrostatic interactions contribute little of stability of barnase.

[1]  A. Fersht,et al.  Strength and co-operativity of contributions of surface salt bridges to protein stability. , 1990, Journal of molecular biology.

[2]  F E Cohen,et al.  Studies of synthetic helical peptides using circular dichroism and nuclear magnetic resonance. , 1990, Journal of molecular biology.

[3]  A. Fersht,et al.  Estimating the contribution of engineered surface electrostatic interactions to protein stability by using double-mutant cycles. , 1990, Biochemistry.

[4]  A. Fersht,et al.  Sequential assignment of the 1H nuclear magnetic resonance spectrum of barnase. , 1990, Biochemistry.

[5]  A. Fersht,et al.  Detection and characterization of a folding intermediate in barnase by NMR , 1990, Nature.

[6]  Andreas Matouschek,et al.  Transient folding intermediates characterized by protein engineering , 1990, Nature.

[7]  D. E. Anderson,et al.  pH-induced denaturation of proteins: a single salt bridge contributes 3-5 kcal/mol to the free energy of folding of T4 lysozyme. , 1990, Biochemistry.

[8]  Alan R. Fersht,et al.  Capping and α-helix stability , 1989, Nature.

[9]  A. Fersht,et al.  Mapping the transition state and pathway of protein folding by protein engineering , 1989, Nature.

[10]  A. Fersht,et al.  Energetics of complementary side-chain packing in a protein hydrophobic core. , 1989, Biochemistry.

[11]  A. Fersht,et al.  Kinetic characterization of the recombinant ribonuclease from Bacillus amyloliquefaciens (barnase) and investigation of key residues in catalysis by site-directed mutagenesis. , 1989, Biochemistry.

[12]  Alan R. Fersht,et al.  Stabilization of protein structure by interaction of α-helix dipole with a charged side chain , 1988, Nature.

[13]  A. Fersht,et al.  Contribution of hydrophobic interactions to protein stability , 1988, Nature.

[14]  M. Perutz,et al.  Stereochemistry of salt‐bridge formation in α‐helices and β‐strands , 1988 .

[15]  R. L. Baldwin,et al.  Helix stabilization by Glu-...Lys+ salt bridges in short peptides of de novo design. , 1987, Proceedings of the National Academy of Sciences of the United States of America.

[16]  A. Fersht,et al.  Rational modification of enzyme catalysis by engineering surface charge , 1987, Nature.

[17]  D. Shortle,et al.  Kinetic and magnetic resonance studies of effects of genetic substitution of a Ca2+-liganding amino acid in staphylococcal nuclease. , 1986, Biochemistry.

[18]  C. Pace Determination and analysis of urea and guanidine hydrochloride denaturation curves. , 1986, Methods in enzymology.

[19]  Thomas A. Kunkel,et al.  Rapid and efficient site-specific mutagenesis without phenotypic selection. , 1985, Proceedings of the National Academy of Sciences of the United States of America.

[20]  R. Hartley,et al.  Cloning, sequencing and transcription of an inactivated copy of Bacillus amyloliquefaciens extracellular ribonuclease (barnase). , 1985, Gene.

[21]  Alan R. Fersht,et al.  The use of double mutants to detect structural changes in the active site of the tyrosyl-tRNA synthetase (Bacillus stearothermophilus) , 1984, Cell.

[22]  A. Warshel,et al.  Calculations of electrostatic interactions in biological systems and in solutions , 1984, Quarterly Reviews of Biophysics.

[23]  Richard R. Ernst,et al.  Coherence transfer by isotropic mixing: Application to proton correlation spectroscopy , 1983 .

[24]  Cyrus Chothia,et al.  Molecular structure of a new family of ribonucleases , 1982, Nature.

[25]  Ad Bax,et al.  Investigation of complex networks of spin-spin coupling by two-dimensional NMR , 1981 .

[26]  K Wüthrich,et al.  A two-dimensional nuclear Overhauser enhancement (2D NOE) experiment for the elucidation of complete proton-proton cross-relaxation networks in biological macromolecules. , 1980, Biochemical and biophysical research communications.

[27]  Richard R. Ernst,et al.  Investigation of exchange processes by two‐dimensional NMR spectroscopy , 1979 .

[28]  M. Perutz Electrostatic effects in proteins. , 1978, Science.

[29]  R. R. Ernst,et al.  Two‐dimensional spectroscopy. Application to nuclear magnetic resonance , 1976 .

[30]  M. Perutz,et al.  Stereochemical basis of heat stability in bacterial ferredoxins and in haemoglobin A2 , 1975, Nature.

[31]  R. Hartley,et al.  Amino-acid sequence of extracellular ribonuclease (barnase) of Bacillus amyloliquefaciens. , 1972, Nature: New biology.

[32]  R. Hartley A reversible thermal transition of the extracellular ribonuclease of Bacillus amyloliquefaciens. , 1968, Biochemistry.