TAILIEUCHUNG - Báo cáo khoa hoc : Homology-modelled structure of the bB2B3-crystallin heterodimer studied by ion mobility and radical probe MS

Ion mobility MS was employed to study the structure of thebB2B3-crystal-lin heterodimer following its detection by ESI-TOF MS. The results dem-onstrate that the heterodimer has a similar cross-section (3 165 A˚ 2 ) and structure to the bB2B2-crystallin homodimer. | IFEBS Journal Homology-modelled structure of the bB2B3-crystallin heterodimer studied by ion mobility and radical probe MS Kevin M. Downard1 Yuichi Kokabu2 Mitsunori Ikeguchi2 and Satoko Akashi2 1 Schoolof Molecular Bioscience University of Sydney Australia 2 Graduate Schoolof Nanobioscience Yokohama City University Japan Keywords heterodimer homology modelling ion mobility MS b-crystallin Correspondence K. Downard Schoolof Molecular Bioscience G-08 The University of Sydney Sydney NSW 2006 Australia Fax 61 2 9351 5858 Tel 61 2 9351 4140 E-mail Received 28 June 2011 revised 24 July 2011 accepted 12 August 2011 doi Ion mobility MS was employed to study the structure of the bB2B3-crystal-lin heterodimer following its detection by ESI-TOF MS. The results demonstrate that the heterodimer has a similar cross-section 3 165 A2 and structure to the bB2B2-crystallin homodimer. Several homology-modelled structures for the bB2B3 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 bB3 subunit are in accord with measured oxidation levels in radical probe MS protein footprinting experiments. The bB2B3 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. Structured digital abstract Beta-crystallin B2 binds to Beta-crystallin B3 by mass spectrometry studies of complexes View interaction Beta-crystallin B2 binds to Beta-crystallin B2 by mass spectrometry studies of complexes View interaction Introduction b-Crystallins are among the most abundant soluble proteins within the lens of the eye in vertebrates 1 . Their ability to associate into dimers tetramers and higher-order aggregates 2 is important for maintaining lens transparency and protecting subunit proteins from oxidative .

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