Hereby, we wish to note our objections to a paper called "Substrate--modulated ADP/ATP--transporter dynamics revealed by NMR relaxation dispersion" by Brüschweiler et al., published in NSMB in 2015 1 .The subject is the yeast mitochondrial ADP/ATP carrier AAC3, which we have studied in great detail ourselves. In particular, we have solved its structure by electron 2 and x--ray crystallography 3 and have studied its interactions with the specific inhibitors atractyloside (ATR) and carboxyatractyloside (CATR) by single--molecule force spectroscopy 4 . In this paper, the authors claim that AAC3 can be refolded to homogeneity from inclusion bodies produced in Escherichia coli by using the detergent dodecyl-phosphocholine (DPC), better known as Foscholine--12 (Anatrace), and that AAC3 is maintained in a folded and active state for the duration of isothermal titration calorimetry (ITC) and NMR experiments.
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