title: Solution structure of the N-terminal domain of the delta subunit of the E. coli ATPsynthase.
abstract: NMR studies of the delta subunit of the Escherichia coli F1F0-ATPsynthase reveal that it consists of an N-terminal six alpha-helix bundle and a less well ordered C terminus. Both domains are part of one of two separate connections between F1 and F0.
authors.forename: S
authors.initials: S
authors.lastname: Wilkens
authors.forename: S D
authors.initials: SD
authors.lastname: Dunn
authors.forename: J
authors.initials: J
authors.lastname: Chandler
authors.forename: F W
authors.initials: FW
authors.lastname: Dahlquist
authors.forename: R A
authors.initials: RA
authors.lastname: Capaldi
mesh_terms: D003198:Computer Simulation; D004926:Escherichia coli / Q000201:enzymology*; D046911:Macromolecular Substances; D009682:Magnetic Resonance Spectroscopy / Q000379:methods; D008961:Models, Structural; D010446:Peptide Fragments / Q000737:chemistry*; D017510:Protein Folding; D017433:Protein Structure, Secondary; D006180:Proton-Translocating ATPases / Q000737:chemistry*; D011994:Recombinant Proteins / Q000737:chemistry; D012984:Software; D012996:Solutions
chemical_list: D046911:Macromolecular Substances; D010446:Peptide Fragments; D011994:Recombinant Proteins; D012996:Solutions; D006180:Proton-Translocating ATPases