Relative tolerance of mesostable and thermostable protein homologs to extensive mutation
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[1] F. Arnold,et al. Protein stability promotes evolvability. , 2006, Proceedings of the National Academy of Sciences of the United States of America.
[2] M. Zaccolo,et al. The effect of high-frequency random mutagenesis on in vitro protein evolution: a study on TEM-1 beta-lactamase. , 1999, Journal of molecular biology.
[3] S Kamtekar,et al. Protein design by binary patterning of polar and nonpolar amino acids. , 1993, Science.
[4] J. Zeikus,et al. Switching substrate preference of thermophilic xylose isomerase from D-xylose to D-glucose by redesigning the substrate binding pocket. , 1991, Proceedings of the National Academy of Sciences of the United States of America.
[5] David Baker,et al. Searching for folded proteins in vitro and in silico. , 2004, European journal of biochemistry.
[6] Chris Pereira,et al. Practical statistics for the biological sciences , 2002 .
[7] G. Böhm,et al. The stability of proteins in extreme environments. , 1998, Current opinion in structural biology.
[8] D. Hilvert,et al. A Strategically Positioned Cation Is Crucial for Efficient Catalysis by Chorismate Mutase* , 2000, The Journal of Biological Chemistry.
[9] D. Hilvert,et al. A simple tagging system for protein encapsulation. , 2006, Journal of the American Chemical Society.
[10] Engineering for redesign , 1994 .
[11] Loren L Looger,et al. Computational Design of a Biologically Active Enzyme , 2004, Science.
[12] P. Karplus,et al. ATOMIC-STRUCTURE OF THE BURIED CATALYTIC POCKET OF ESCHERICHIA-COLI CHORISMATE MUTASE. , 1995 .
[13] Christoph Adami,et al. Stability and the evolvability of function in a model protein. , 2004, Biophysical journal.
[14] W. V. van Zyl,et al. Cold adaptation of xylose isomerase from Thermus thermophilus through random PCR mutagenesis. Gene cloning and protein characterization. , 2002, European journal of biochemistry.
[15] V. Eijsink,et al. Rational engineering of enzyme stability. , 2004, Journal of biotechnology.
[16] Boris Steipe,et al. Consensus-based engineering of protein stability: from intrabodies to thermostable enzymes. , 2004, Methods in enzymology.
[17] Donald Hilvert,et al. Searching sequence space for protein catalysts , 2001, Proceedings of the National Academy of Sciences of the United States of America.
[18] Donald Hilvert,et al. New enzymes from combinatorial library modules. , 2004, Methods in enzymology.
[19] M Vihinen,et al. Relationship of protein flexibility to thermostability. , 1987, Protein engineering.
[20] D. Hilvert,et al. Exploring sequence constraints on an interhelical turn using in vivo selection for catalytic activity , 1998, Protein science : a publication of the Protein Society.
[21] D. Hilvert,et al. A small, thermostable, and monofunctional chorismate mutase from the archaeon Methanococcus jannaschii. , 1998, Biochemistry.
[22] R. Siegel,et al. Generation of large libraries of random mutants in Bacillus subtilis by PCR-based plasmid multimerization. , 1997, BioTechniques.
[23] Miguel Ángel Martínez,et al. Exploring the functional robustness of an enzyme by in vitro evolution. , 1996, The EMBO journal.
[24] L. H. Bradley,et al. Protein design by binary patterning of polar and nonpolar amino acids. , 1993, Methods in molecular biology.
[25] B. Ganem,et al. A genetically engineered monofunctional chorismate mutase , 1990 .
[26] G A Petsko,et al. Adjustment of conformational flexibility is a key event in the thermal adaptation of proteins. , 1998, Proceedings of the National Academy of Sciences of the United States of America.
[27] Juno Choe,et al. Protein tolerance to random amino acid change. , 2004, Proceedings of the National Academy of Sciences of the United States of America.
[28] G. Georgiou,et al. Quantitative analysis of the effect of the mutation frequency on the affinity maturation of single chain Fv antibodies. , 2000, Proceedings of the National Academy of Sciences of the United States of America.
[29] Frances H Arnold,et al. Why high-error-rate random mutagenesis libraries are enriched in functional and improved proteins. , 2004, Journal of molecular biology.
[30] D. Hilvert,et al. Conversion of a PLP-dependent racemase into an aldolase by a single active site mutation. , 2003, Journal of the American Chemical Society.
[31] W. Lim,et al. Deciphering the message in protein sequences: tolerance to amino acid substitutions. , 1990, Science.
[32] J. Szostak,et al. Constructing high complexity synthetic libraries of long ORFs using in vitro selection. , 2000, Journal of molecular biology.
[33] Manuela Zaccolo,et al. The Effect of High-frequency Random Mutagenesis on in Vitro Protein Evolution : A Study on TEM-1 b-Lactamase , 1998 .
[34] G. Petsko. Structural basis of thermostability in hyperthermophilic proteins, or "there's more than one way to skin a cat". , 2001, Methods in enzymology.
[35] D. Hilvert,et al. Probing enzyme quaternary structure by combinatorial mutagenesis and selection , 1998, Protein science : a publication of the Protein Society.
[36] Keith A. Powell,et al. Directed Evolution and Biocatalysis. , 2001, Angewandte Chemie.
[37] M. Lehmann,et al. Engineering proteins for thermostability: the use of sequence alignments versus rational design and directed evolution. , 2001, Current opinion in biotechnology.
[38] Donald Hilvert,et al. Investigating and Engineering Enzymes by Genetic Selection. , 2001, Angewandte Chemie.
[39] F. Arnold. Design by Directed Evolution , 1998 .
[40] F. Christians,et al. Tolerance of different proteins for amino acid diversity , 1996, Molecular Diversity.
[41] D. Hilvert,et al. Simultaneous optimization of enzyme activity and quaternary structure by directed evolution , 2005, Protein science : a publication of the Protein Society.
[42] D. Hilvert,et al. Exploring the active site of chorismate mutase by combinatorial mutagenesis and selection: the importance of electrostatic catalysis. , 1996, Proceedings of the National Academy of Sciences of the United States of America.
[43] Georg E. Schulz,et al. Degeneracy of the information contained in amino acid sequences: Evidence from overlaid genes , 1979, Journal of Molecular Evolution.
[44] D. Hilvert,et al. Redesigning enzyme topology by directed evolution. , 1998, Science.
[45] Christoph Adami,et al. Thermodynamic prediction of protein neutrality. , 2004, Proceedings of the National Academy of Sciences of the United States of America.