PMID:14706821
| Citation |
Dmitriev, OY, Altendorf, K and Fillingame, RH (2004) Subunit A of the E. coli ATP synthase: reconstitution and high resolution NMR with protein purified in a mixed polarity solvent. FEBS Lett. 556:35-8 |
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| Abstract |
Subunit a of the Escherichia coli ATP synthase, a 30 kDa integral membrane protein, was purified to homogeneity by a novel procedure incorporating selective extraction into a monophasic mixture of chloroform, methanol and water, followed by Ni-NTA chromatography in the mixed solvent. Pure subunit a was reconstituted with subunits b and c and phospholipids to form a functional proton-translocating unit. Nuclear magnetic resonance (NMR) spectra of the pure subunit a in the mixed solvent show good chemical shift dispersion and demonstrate the potential of the solvent mixture for NMR studies of the large membrane proteins that are currently intractable in aqueous detergent solutions. |
| Links | |
| Keywords |
Amino Acid Sequence; Bacterial Proton-Translocating ATPases; Chloroform/chemistry; Chromatography, Agarose/methods; Escherichia coli/enzymology; Escherichia coli/genetics; Escherichia coli Proteins/chemistry; Escherichia coli Proteins/genetics; Escherichia coli Proteins/isolation & purification; Membrane Proteins/chemistry; Membrane Proteins/isolation & purification; Methanol/chemistry; Mitochondrial Proton-Translocating ATPases/chemistry; Mitochondrial Proton-Translocating ATPases/genetics; Mitochondrial Proton-Translocating ATPases/isolation & purification; Molecular Sequence Data; Nuclear Magnetic Resonance, Biomolecular; Protein Structure, Secondary; Protein Subunits/chemistry; Protein Subunits/genetics; Protein Subunits/isolation & purification; Proteolipids/metabolism; Protons; Solvents/chemistry; Water/chemistry |
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