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Issue 2, 2015
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Structural characterization of holo- and apo-myoglobin in the gas phase by ultraviolet photodissociation mass spectrometry

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Abstract

Ultraviolet photodissociation (UVPD) mass spectrometry is employed to investigate the structure of holo-myoglobin as well as its apo form transferred to the gas phase by native electrospray. UVPD provided insight into the stability of native structural elements of holo-myoglobin. The fragmentation yields from UVPD showed the greatest overall correlation with B-factors generated from the crystal structure of apo-myoglobin, particularly for the more disordered loop regions. Solvent accessibility measurements also showed some correlation with the UVPD fragmentation of holo-myoglobin. Comparison of UVPD of holo- and apo-myoglobin revealed similarities in fragmentation yields, particularly for the lower charge states (8 and 9+). Both holo- and apo-myoglobin exhibited low fragmentation yields for the AGH helical core, whereas regions known to interact with the heme show suppressed fragmentation for holo-myoglobin. The fragment yields from HCD showed the lowest correlation with B-factor values and rather reflected preferential charge-directed backbone cleavages.

Graphical abstract: Structural characterization of holo- and apo-myoglobin in the gas phase by ultraviolet photodissociation mass spectrometry

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Publication details

The article was received on 18 Oct 2014, accepted on 26 Nov 2014 and first published on 26 Nov 2014


Article type: Edge Article
DOI: 10.1039/C4SC03200D
Citation: Chem. Sci., 2015,6, 1324-1333
  • Open access: Creative Commons BY-NC license
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    Structural characterization of holo- and apo-myoglobin in the gas phase by ultraviolet photodissociation mass spectrometry

    M. B. Cammarata and J. S. Brodbelt, Chem. Sci., 2015, 6, 1324
    DOI: 10.1039/C4SC03200D

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