title: Towards an understanding of structure-function relationships of elongation factor Tu.
abstract: In light of the recently determined structure of elongation factor Tu, and taking into account chemical studies mapping functional sites, a number of residues have been selected for site-directed mutagenesis studies. Gly94, Gly126, His66, His118, Lys89 and Asp90 have each been point-mutated. Preliminary in vitro characterization data are presented.
authors.affiliation: Department of Biostructural Chemistry, Aarhus University, Denmark.
authors.forename: O
authors.initials: O
authors.lastname: Wiborg
authors.forename: C
authors.initials: C
authors.lastname: Andersen
authors.forename: C R
authors.initials: CR
authors.lastname: Knudsen
authors.forename: T J
authors.initials: TJ
authors.lastname: Kristensen
authors.forename: B F
authors.initials: BF
authors.lastname: Clark
mesh_terms: D000596:Amino Acids / Q000032:analysis / Q000378:metabolism; D004926:Escherichia coli / Q000378:metabolism; D008958:Models, Molecular; D016297:Mutagenesis, Site-Directed; D010444:Peptide Elongation Factor Tu / Q000737:chemistry* / Q000235:genetics / Q000502:physiology*; D017354:Point Mutation; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D013329:Structure-Activity Relationship
chemical_list: D000596:Amino Acids; D010444:Peptide Elongation Factor Tu