Quaternary structure of <Emphasis Type="Italic">Artemia</Emphasis> haemoglobin II: analysis of T and C polymer alignment and interpolymer interface |
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Authors: | David T Chyou Vincent L Rawle Clive NA Trotman |
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Institution: | (1) Department of Biochemistry, University of Otago, Dunedin, New Zealand |
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Abstract: | Background The brine shrimp Artemia expresses four different types of haemoglobin subunits namely C1, C2, T1 and T2. Two of these four subunits dimerize in different
combinations to produce the three isoforms of the heterodimeric Artemia haemoglobin: HbI (C1 and C2), HbII (C1 and T2) and HbIII (T1 and T2). Previous biochemical, biophysical and computational
analyses demonstrate that the T and C polymers are rings of nine concatenated globin domains, which are covalently joined
by interdomain linkers. Two such rings stacked coaxially give the functional molecule. This research aimed to construct a
quaternary structural model of Artemia HbII that shows the interpolymer interface and domain-domain alignment, using the MS3D (mass spectrometry for three dimensional
analysis) approach. This involved introducing chemical crosslinks between the two polymers, cleaving with trypsin and analyzing
the resulting products by mass spectrometry. This was followed by computational analysis of the mass spectrometry data using
the program SearchXlinks to identify putatively crosslinked peptides. |
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Keywords: | |
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