title: Homology-modelled structure of the βB2B3-crystallin heterodimer studied by ion mobility and radical probe MS.
abstract: Ion mobility MS was employed to study the structure of the βB2B3-crystallin heterodimer following its detection by ESI-TOF MS. The results demonstrate that the heterodimer has a similar cross-section (3 165 Å(2)) and structure to the βB2B2-crystallin homodimer. Several homology-modelled structures for the βB2B3 heterodimer were constructed and assessed in terms of their calculated collision cross-sections and whether the solvent accessibilities of reactive amino acid side chains throughout the βB3 subunit are in accord with measured oxidation levels in radical probe MS protein footprinting experiments. The βB2B3 heterodimer AD model provides the best representation of the heterodimer's structure overall following a consideration of both the ion mobility and radical probe MS data.
authors.affiliation: School of Molecular Bioscience, University of Sydney, Sydney, Australia. k.downard@sydney.edu.au
authors.forename: Kevin M
authors.initials: KM
authors.lastname: Downard
authors.forename: Yuichi
authors.initials: Y
authors.lastname: Kokabu
authors.forename: Mitsunori
authors.initials: M
authors.lastname: Ikeguchi
authors.forename: Satoko
authors.initials: S
authors.lastname: Akashi
mesh_terms: D000595:Amino Acid Sequence; D003459:Crystallins / Q000737:chemistry*; D018360:Crystallography, X-Ray; D019281:Dimerization; D015335:Molecular Probes; D008969:Molecular Sequence Data; D010084:Oxidation-Reduction; D011487:Protein Conformation; D017386:Sequence Homology, Amino Acid; D021241:Spectrometry, Mass, Electrospray Ionization / Q000379:methods*
chemical_list: D003459:Crystallins; D015335:Molecular Probes