title: Enhanced protein thermostability from designed mutations that interact with alpha-helix dipoles.
abstract: Two different genetically engineered amino-acid substitutions designed to interact with alpha-helix dipoles in T4 lysozyme are shown to increase the thermal stability of the protein. Crystallographic analyses of the mutant lysozyme structures suggest that the stabilization is due to electrostatic interaction and does not require precise hydrogen bonding between the substituted amino acid and the end of the alpha-helix.
authors.affiliation: Institute of Molecular Biology, University of Oregon, Eugene 97403.
authors.forename: H
authors.initials: H
authors.lastname: Nicholson
authors.forename: W J
authors.initials: WJ
authors.lastname: Becktel
authors.forename: B W
authors.initials: BW
authors.lastname: Matthews
mesh_terms: D001224:Aspartic Acid / Q000378:metabolism*; D001665:Binding Sites; D055598:Chemical Phenomena; D002621:Chemistry; D003460:Crystallization; D004268:DNA-Binding Proteins / Q000378:metabolism*; D005818:Genetic Engineering / Q000379:methods; D006863:Hydrogen-Ion Concentration; D009113:Muramidase / Q000235:genetics / Q000378:metabolism*; D009154:Mutation; D013329:Structure-Activity Relationship; D013604:T-Phages / Q000201:enzymology; D013696:Temperature; D013816:Thermodynamics
chemical_list: D004268:DNA-Binding Proteins; D001224:Aspartic Acid; D009113:Muramidase