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Utilizing Ion Mobility-Mass Spectrometry to Investigate the Unfolding Pathway of Cu/Zn Superoxide Dismutase

ABSTRACT: IMS-MS data for Cu/Zn-Superoxide Dismutase (from bovine erythrocytes). Experiments were conducted on two different IMS platforms (DTIMS and TIMS) to compare the CCS values obtained under different types of IMS. Three separate solution conditions were used for the DTIMS data in order to obtain CCS values for the native, holo-dimeric protein, the holo-monomer, and the apo-monomer. Native conditions (30 mM ammonium acetate) were used to assess the native protein structure (holo-dimer). Holo-monomer formation was promoted by addition of 30% acetonitrile and 100 uM formic acid, while apo-monomer formation was promoted by addition of 30% acetonitrile and 0.1% formic acid.

INSTRUMENT(S): timsTOF (Bruker instrument model), 6560 Ion Mobility Q-ToF (Agilent instrument model)

ORGANISM(S): Bovine (from Erythrocytes)

SUBMITTER: Erin Baker

PROVIDER: MSV000086204 | MassIVE |

REPOSITORIES: MassIVE

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