Human S100b protein: Formation of a tetramer from synthetic calcium-binding site peptides
作者： Craig Donaldson , Kathryn R. Barber , Gary S. Shaw , Cyril M. Kay
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摘要: Human brain S100b protein is a unique calcium-binding comprised of two identical 91-amino acid polypeptide chains that each contain proposed helix-loop-helix (EF-hand) sites. In order to probe the assembly four sites in S100b, peptide N-terminal 46 residues was synthesized and studied by CD 1H NMR spectroscopies as function concentration temperature. At relatively high concentrations absence calcium, exhibited significant proportion α-helix (45%). Decreasing led loss monitored spectroscopy coincident changes spectrum. These were also observed temperature where it Tm lowered approximately 14 °C with 17-fold decrease concentration. Sedimentation equilibrium studies used determine formed tetramer solution calcium. It this tetrameric fold occurs result interaction portions all
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