title: Modification of the stability of phospholipase A2 by charge engineering.
abstract: Electrostatic interactions play an important role in stabilizing the folded conformation of globular proteins. Here we predict the change in stability of charge engineered mutants, construct these mutants and compare the predicted change in stability with that observed. The change in stability was correctly predicted for two of the three mutants and the factors responsible for the discrepancy between observation and prediction for the third mutant are discussed.
authors.affiliation: Protein Engineering Department, AFRC Institute of Food Research, Reading Laboratory, Shinfield, UK.
authors.forename: R W
authors.initials: RW
authors.lastname: Pickersgill
authors.forename: I G
authors.initials: IG
authors.lastname: Sumner
authors.forename: M E
authors.initials: ME
authors.lastname: Collins
authors.forename: J
authors.initials: J
authors.lastname: Warwicker
authors.forename: B
authors.initials: B
authors.lastname: Perry
authors.forename: K M
authors.initials: KM
authors.lastname: Bhat
authors.forename: P W
authors.initials: PW
authors.lastname: Goodenough
mesh_terms: D004795:Enzyme Stability; D019791:Guanidine; D006146:Guanidines; D006863:Hydrogen-Ion Concentration; D008958:Models, Molecular; D016296:Mutagenesis; D010741:Phospholipases A / Q000737:chemistry* / Q000235:genetics; D054467:Phospholipases A2; D011487:Protein Conformation; D011489:Protein Denaturation; D012984:Software; D014961:X-Ray Diffraction
chemical_list: D006146:Guanidines; D010741:Phospholipases A; D054467:Phospholipases A2; D019791:Guanidine