title: Use of Random and Site-Directed Mutagenesis to Probe Protein Structure-Function Relationships: Applied Techniques in the Study of Helicobacter pylori.
abstract: Mutagenesis is a valuable tool to examine the structure-function relationships of bacterial proteins. As such, a wide variety of mutagenesis techniques and strategies have been developed. This chapter details a selection of random mutagenesis methods and site-directed mutagenesis procedures that can be applied to an array of bacterial species. Additionally, the direct application of the techniques to study the Helicobacter pylori Ferric Uptake Regulator (Fur) protein is described. The varied approaches illustrated herein allow the robust investigation of the structural-functional relationships within a protein of interest.
authors.affiliation: Department of Microbiology and Immunology, Uniformed Services University of the Health Sciences, 4301 Jones Bridge Road, Bethesda, MD, 20814, USA.
authors.forename: Jeannette M
authors.initials: JM
authors.lastname: Whitmire
authors.affiliation: Department of Microbiology and Immunology, Uniformed Services University of the Health Sciences, 4301 Jones Bridge Road, Bethesda, MD, 20814, USA. douglas.merrell@usuhs.edu.
authors.forename: D Scott
authors.initials: DS
authors.lastname: Merrell
mesh_terms: D001426:Bacterial Proteins / Q000235:genetics*; D016480:Helicobacter pylori / Q000235:genetics*; D007501:Iron / Q000378:metabolism; D016296:Mutagenesis / Q000235:genetics*; D016297:Mutagenesis, Site-Directed / Q000379:methods; D012097:Repressor Proteins / Q000235:genetics; D013329:Structure-Activity Relationship
chemical_list: D001426:Bacterial Proteins; D012097:Repressor Proteins; D007501:Iron
keywords: Bacterial mutagenesis; Protein analysis; Random mutagenesis; Site-directed mutagenesis; Structure–function