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Homology‐modelled structure of the βB2B3‐crystallin heterodimer studied by ion mobility and radical probe MS
Author(s) -
Downard Kevin M.,
Kokabu Yuichi,
Ikeguchi Mitsunori,
Akashi Satoko
Publication year - 2011
Publication title -
the febs journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.981
H-Index - 204
eISSN - 1742-4658
pISSN - 1742-464X
DOI - 10.1111/j.1742-4658.2011.08309.x
Subject(s) - chemistry , mass spectrometry , protein subunit , ion mobility spectrometry , ion , footprinting , crystallin , biophysics , crystallography , biochemistry , chromatography , organic chemistry , dna , base sequence , biology , gene
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. Structured digital abstract• Beta‐crystallin B2 binds to Beta‐crystallinB3 by mass spectrometry studies of complexes (View interaction ) • Beta‐crystallinB2 binds to Beta‐crystallinB2 by mass spectrometry studies of complexes (View interaction )