Surface electrostatic interactions contribute little of stability of barnase.
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A. Fersht | M. Bycroft | D. Sali | Dasa Sali
[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.