title: The use of forced protein evolution to investigate and improve stability of family 10 xylanases. The production of Ca2+-independent stable xylanases.
authors.affiliation: Structural Biology Laboratory, Department of Chemistry, University of York, Heslington, York YO10 5YW, UK.
authors.forename: Simon R
authors.initials: SR
authors.lastname: Andrews
authors.forename: Edward J
authors.initials: EJ
authors.lastname: Taylor
authors.forename: Gavin
authors.initials: G
authors.lastname: Pell
authors.forename: Florence
authors.initials: F
authors.lastname: Vincent
authors.forename: Valérie M-A
authors.initials: VM
authors.lastname: Ducros
authors.forename: Gideon J
authors.initials: GJ
authors.lastname: Davies
authors.forename: Jeremy H
authors.initials: JH
authors.lastname: Lakey
authors.forename: Harry J
authors.initials: HJ
authors.lastname: Gilbert
mesh_terms: D001665:Binding Sites; D002118:Calcium / Q000378:metabolism / Q000494:pharmacology*; D020633:Cellvibrio / Q000201:enzymology*; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D003460:Crystallization; D019020:Directed Molecular Evolution; D004220:Disulfides / Q000737:chemistry; D004351:Drug Resistance; D004492:Edetic Acid / Q000494:pharmacology; D043364:Endo-1,4-beta Xylanases; D004795:Enzyme Stability; D004926:Escherichia coli / Q000235:genetics; D006358:Hot Temperature; D006860:Hydrogen Bonding; D016296:Mutagenesis; D016297:Mutagenesis, Site-Directed; D010447:Peptide Hydrolases / Q000494:pharmacology; D016133:Polymerase Chain Reaction; D017510:Protein Folding; D011994:Recombinant Proteins; D013329:Structure-Activity Relationship; D013438:Sulfhydryl Compounds / Q000032:analysis; D013816:Thermodynamics; D014995:Xylosidases / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism*
chemical_list: D004220:Disulfides; D011994:Recombinant Proteins; D013438:Sulfhydryl Compounds; D004492:Edetic Acid; D014995:Xylosidases; D043364:Endo-1,4-beta Xylanases; D010447:Peptide Hydrolases; D002118:Calcium