1997
Speeding up protein folding: mutations that increase the rate at which Rop folds and unfolds by over four orders of magnitude
Munson M, Anderson K, Regan L. Speeding up protein folding: mutations that increase the rate at which Rop folds and unfolds by over four orders of magnitude. Structure 1997, 2: 77-87. PMID: 9080201, DOI: 10.1016/s1359-0278(97)00008-4.Peer-Reviewed Original Research
1995
Expression of Human Cyclophilin‐40 and the Effect of the His141→Trp Mutation on Catalysis and Cyclosporin A Binding
Hoffmann K, Kakalis L, Anderson K, Armitage I, Handschumacher R. Expression of Human Cyclophilin‐40 and the Effect of the His141→Trp Mutation on Catalysis and Cyclosporin A Binding. The FEBS Journal 1995, 229: 188-193. PMID: 7744028, DOI: 10.1111/j.1432-1033.1995.0188l.x.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid IsomerasesBase SequenceBinding SitesCarrier ProteinsCyclophilin DCyclophilinsCyclosporineEnzyme ActivationEscherichia coliHumansMagnetic Resonance SpectroscopyModels, MolecularMolecular Sequence DataMutagenesis, Site-DirectedPeptidylprolyl IsomeraseProtein BindingRecombinant ProteinsConceptsCyP-40Isomerase activityPeptidyl-prolyl cis-trans isomerase activityHuman cyclophilin-40PGEX-3X expression vectorSite-directed mutagenesisMutant proteinsCyclophilin 40Intrinsic isomerase activityNMR difference spectroscopySuccinyl-AlaExpression vectorHistidine residuesEscherichia coliTryptophan residuesProteinCyclophilinMolecular modellingAla-ProResiduesGel filtrationWeak affinityBindingHigh affinityAffinity matrix