Extreme functional sensitivity to conservative amino acid changes on enzyme exteriors.
暂无分享,去创建一个
[1] N. Guex,et al. SWISS‐MODEL and the Swiss‐Pdb Viewer: An environment for comparative protein modeling , 1997, Electrophoresis.
[2] T. Jukes. Non-Darwinian Evolution , 2001 .
[3] Laurent Maveyraud,et al. Crystal Structure of 6Alpha-Hydroxymethylpenicillanate Complexed to the Tem-1 Beta-Lactamase from Escherichia Coli: Evidence on the Mechanism of Action of a Novel Inhibitor Designed by a Computer-Aided Process , 1996 .
[4] Robert T. Sauer,et al. Cooperatively folded proteins in random sequence libraries , 1995, Nature Structural Biology.
[5] R. Sauer,et al. Sequence space, folding and protein design. , 1996, Current opinion in structural biology.
[6] H. Bedouelle,et al. Mapping the stability determinants of bacterial tyrosyl transfer RNA synthetases by an experimental evolutionary approach. , 1993, Journal of molecular biology.
[7] M. Kimura,et al. Recent development of the neutral theory viewed from the Wrightian tradition of theoretical population genetics. , 1991, Proceedings of the National Academy of Sciences of the United States of America.
[8] C Chothia,et al. Structural determinants in the sequences of immunoglobulin variable domain. , 1998, Journal of molecular biology.
[9] A M Lesk,et al. Interior and surface of monomeric proteins. , 1987, Journal of molecular biology.
[10] K. Young,et al. AmpC and AmpH, proteins related to the class C beta-lactamases, bind penicillin and contribute to the normal morphology of Escherichia coli , 1997, Journal of bacteriology.
[11] Venema,et al. Engineering of the Lactococcus lactis serine proteinase by construction of hybrid enzymes. , 1991, Protein engineering.
[12] A. Fersht,et al. An irregular beta-bulge common to a group of bacterial RNases is an important determinant of stability and function in barnase. , 1999, Journal of molecular biology.
[13] K. Sugimoto,et al. Recovery of active beta-lactamases from Proteus vulgaris and RTEM-1 hybrid by random mutagenesis by using a dnaQ strain of Escherichia coli , 1996, Antimicrobial agents and chemotherapy.
[14] P M Bennett,et al. Molecular basis of beta-lactamase induction in bacteria , 1993, Antimicrobial Agents and Chemotherapy.
[15] H. Zuber,et al. Structure and function of L-lactate dehydrogenases from thermophilic and mesophilic bacteria, X. Analysis of structural elements responsible for the differences in thermostability and activation by fructose 1,6-bisphosphate in the lactate dehydrogenases from B. stearothermophilus and B. caldolyticus , 1990, Biological chemistry Hoppe-Seyler.
[16] J. Wild,et al. Reconstruction of an enzyme by domain substitution effectively switches substrate specificity , 1989, Nature.
[17] T. Sawai,et al. Nucleotide sequence and characterization of a carbenicillin-hydrolyzing penicillinase gene from Proteus mirabilis , 1991, Journal of bacteriology.
[18] Jeffrey Miller,et al. Genetic Studies of Lac Repressor: 4000 Single Amino Acid Substitutions and Analysis of the Resulting Phenotypes on the Basis of the Protein Structure , 1996, German Conference on Bioinformatics.
[19] W. Lim,et al. Deciphering the message in protein sequences: tolerance to amino acid substitutions. , 1990, Science.
[20] A. Riggs,et al. Active human-yeast chimeric phosphoglycerate kinases engineered by domain interchange , 1986, Science.
[21] Robert M. Stroud,et al. A designed four helix bundle protein with native-like structure , 1997, Nature Structural Biology.
[22] R. Sauer,et al. Combinatorial cassette mutagenesis as a probe of the informational content of protein sequences. , 1988, Science.
[23] B. Matthews,et al. Studies on protein stability with T4 lysozyme. , 1995, Advances in protein chemistry.
[24] Marc Ostermeier,et al. A combinatorial approach to hybrid enzymes independent of DNA homology , 1999, Nature Biotechnology.
[25] J. Petrosino,et al. Amino acid sequence determinants of beta-lactamase structure and activity. , 1996, Journal of molecular biology.
[26] Brian W. Matthews,et al. Ancestral lysozymes reconstructed, neutrality tested, and thermostability linked to hydrocarbon packing , 1990, Nature.
[27] A. Fersht,et al. Insertion in barnase of a loop sequence from ribonuclease T1. Investigating sequence and structure alignments by protein engineering. , 1994, European journal of biochemistry.
[28] M. Perutz,et al. Molecular Pathology of Human Haemoglobin , 1968, Nature.
[29] M. Kimura. Evolutionary Rate at the Molecular Level , 1968, Nature.
[30] Peter S. Shenkin,et al. Amino Acid Sequence Determinants of β-Lactamase Structure and Activity , 1996 .
[31] G. Gonnet,et al. Exhaustive matching of the entire protein sequence database. , 1992, Science.
[32] A. Fersht,et al. Active barnase variants with completely random hydrophobic cores. , 1996, Proceedings of the National Academy of Sciences of the United States of America.
[33] D. Baker,et al. Functional rapidly folding proteins from simplified amino acid sequences , 1997, Nature Structural Biology.
[34] S. Bouvier,et al. Systematic mutation of bacteriophage T4 lysozyme. , 1991, Journal of molecular biology.
[35] A. Fersht,et al. A search for single substitutions that eliminate enzymatic function in a bacterial ribonuclease. , 1998, Biochemistry.
[36] K. Hayashi,et al. Construction of Chimeric β-Glucosidases with Improved Enzymatic Properties (*) , 1995, The Journal of Biological Chemistry.
[37] W. P. Schneider,et al. Procedure for production of hybrid genes and proteins and its use in assessing significance of amino acid differences in homologous tryptophan synthetase alpha polypeptides. , 1981, Proceedings of the National Academy of Sciences of the United States of America.
[38] T. Jukes,et al. The neutral theory of molecular evolution. , 2000, Genetics.
[39] J. C. Kendrew,et al. Structure and function of haemoglobin: II. Some relations between polypeptide chain configuration and amino acid sequence , 1965 .
[40] J M Ghuysen,et al. A standard numbering scheme for the class A beta-lactamases. , 1991, The Biochemical journal.
[41] D Baker,et al. Simplified proteins: minimalist solutions to the 'protein folding problem'. , 1998, Current opinion in structural biology.
[42] J H Miller,et al. Genetic studies of the lac repressor. I. Correlation of mutational sites with specific amino acid residues: construction of a colinear gene-protein map. , 1977, Journal of molecular biology.
[43] T C Terwilliger,et al. In vivo characterization of mutants of the bacteriophage f1 gene V protein isolated by saturation mutagenesis. , 1994, Journal of molecular biology.
[44] Steven A. Benner,et al. Reconstructing the evolutionary history of the artiodactyl ribonuclease superfamily , 1995, Nature.
[45] R. Sauer,et al. Protein folding from a combinatorial perspective. , 1996, Folding & design.
[46] K. Sugimoto,et al. Recovery of Active b-Lactamases from Proteus vulgaris and RTEM-1 Hybrid by Random Mutagenesis by Using a dnaQ Strain of Escherichia coli , 1996 .
[47] S. Benkovic,et al. Assembly of an active enzyme by the linkage of two protein modules. , 1997, Proceedings of the National Academy of Sciences of the United States of America.
[48] A. G. Day,et al. 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. , 1993, Journal of molecular biology.
[49] W. Stemmer,et al. DNA shuffling of a family of genes from diverse species accelerates directed evolution , 1998, Nature.
[50] P. Moews,et al. Beta-lactamase of Bacillus licheniformis 749/C. Refinement at 2 A resolution and analysis of hydration. , 1991, Journal of molecular biology.
[51] A. Fersht,et al. Subsite binding in an RNase: structure of a barnase-tetranucleotide complex at 1.76-A resolution. , 1994, Biochemistry.
[52] M. Lehmann,et al. From DNA sequence to improved functionality: using protein sequence comparisons to rapidly design a thermostable consensus phytase. , 2000, Protein engineering.
[53] Marc Ostermeier,et al. Finding Cinderella's slipper—proteins that fit , 1999, Nature Biotechnology.
[54] L. H. Bradley,et al. Protein design by binary patterning of polar and nonpolar amino acids. , 1993, Methods in molecular biology.