Strength and co-operativity of contributions of surface salt bridges to protein stability.

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

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

[3]  A. Fersht,et al.  Strategy for analysing the co-operativity of intramolecular interactions in peptides and proteins. , 1990, Journal of molecular biology.

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

[5]  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.

[6]  Philip R. Evans,et al.  Structural basis of the allosteric behaviour of phosphofructokinase , 1990, Nature.

[7]  B. Matthews,et al.  A mutant T4 lysozyme (Val 131 → Ala) designed to increase thermostability by the reduction of strain within an α‐helix , 1990, Proteins.

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

[9]  R. Hartley,et al.  Barnase and barstar: two small proteins to fold and fit together. , 1989, Trends in biochemical sciences.

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

[11]  C. Richardson,et al.  Selective inactivation of the exonuclease activity of bacteriophage T7 DNA polymerase by in vitro mutagenesis. , 1989, The Journal of biological chemistry.

[12]  B. Matthews,et al.  Enhanced protein thermostability from designed mutations that interact with α-helix dipoles , 1990, Nature.

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

[14]  A violent birth for Mercury , 1988, Nature.

[15]  J. Dunn,et al.  ompT encodes the Escherichia coli outer membrane protease that cleaves T7 RNA polymerase during purification , 1988, Journal of bacteriology.

[16]  J. Sayers,et al.  5'-3' exonucleases in phosphorothioate-based oligonucleotide-directed mutagenesis. , 1988, Nucleic acids research.

[17]  G. Petsko,et al.  Weakly polar interactions in proteins. , 1988, Advances in protein chemistry.

[18]  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.

[19]  R J Leatherbarrow,et al.  Structure-activity relationships in engineered proteins: analysis of use of binding energy by linear free energy relationships. , 1987, Biochemistry.

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

[21]  A. Horovitz,et al.  Non-additivity in protein-protein interactions. , 1987, Journal of molecular biology.

[22]  C. Richardson,et al.  DNA sequence analysis with a modified bacteriophage T7 DNA polymerase. , 1987, Proceedings of the National Academy of Sciences of the United States of America.

[23]  F. William Studier,et al.  T7 lysozyme inhibits transcription by T7 RNA polymerase , 1987, Cell.

[24]  R. Hartley,et al.  Expression of Bacillus amyloliquefaciens extracellular ribonuclease (barnase) in Escherichia coli following an inactivating mutation. , 1987, Gene.

[25]  M. Sundaralingam,et al.  Ion pairs in alpha helices , 1987, Proteins.

[26]  F. Studier,et al.  Use of bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genes. , 1986, Journal of molecular biology.

[27]  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.

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

[29]  G. K. Ackers,et al.  EFFECTS OF SITE-SPECIFIC AMINO ACID MODIFICATION ON PROTEIN INTERACTIONS AND BIOLOGICAL FUNCTION , 1985 .

[30]  G. Rose,et al.  Turns in peptides and proteins. , 1985, Advances in protein chemistry.

[31]  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.

[32]  Harold A. Scheraga,et al.  Helix-coil stability constants for the naturally occurring amino acids in water. 22. Histidine parameters from random poly[(hydroxybutyl)glutamine-co-L-histidine] , 1984 .

[33]  A. Fersht,et al.  Direct observation of complexes formed between recA protein and a fluorescent single-stranded deoxyribonucleic acid derivative. , 1982, Biochemistry.

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

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

[36]  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.

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

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

[39]  A. C. Chang,et al.  Construction and characterization of amplifiable multicopy DNA cloning vehicles derived from the P15A cryptic miniplasmid , 1978, Journal of bacteriology.

[40]  P. Y. Chou,et al.  Empirical predictions of protein conformation. , 1978, Annual review of biochemistry.

[41]  A. Fersht.  Enzyme structure and mechanism , 1977 .

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

[43]  M. Inouye,et al.  Bacteriophage T7 lysozyme is an N-acetylmuramyl-L-alanine amidase. , 1973, The Journal of biological chemistry.

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