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The affinity purification and characterization of ATP synthase complexes from mitochondria.
Michael J Runswick, John V Bason, Martin G Montgomery, Graham C Robinson, Ian M Fearnley, John E Walker
Aug 11, 2017
The mitochondrial F₁-ATPase inhibitor protein, IF₁, inhibits the hydrolytic, but not the synthetic activity of the F-ATP synthase, and requires the hydrolysis of ATP to form the inhibited complex. In this complex, the α-helical...
Heat treatment of thioredoxin fusions increases the purity of α-helical transmembrane protein constructs.
Membrane proteins play key roles in cellular signaling and transport, represent the majority of drug targets, and are implicated in many diseases. Their relevance renders them important subjects for structural, biophysical, and...
Heat treatment Membrane Proteins Protein purification thioredoxin ATP Synthetase Complexes Bacterial Proteins Cloning Molecular Cystic Fibrosis Transmembrane Conductance Regulator Escherichia coli Fusobacteria Gene Expression Genetic Vectors Hot Temperature Humans Models Molecular Protein Conformation alpha-Helical Protein Conformation beta-Strand Protein Interaction Domains and Motifs Protein Subunits Recombinant Fusion Proteins Solubility Thioredoxins
The structure of the catalytic domain of the ATP synthase from Mycobacterium smegmatis is a target for developing antitubercular drugs.
Alice Tianbu Zhang, Martin G Montgomery, Andrew GW Leslie, Gregory M Cook, John E Walker
Feb 07, 2019