Src homology domain-mediated protein interactions Lindfors, H.E.

The GFP-SH32 construct is also found to localize to focal adhesions, although to a lesser extent than the double SH2 domains (Fig. 7.1b), reflecting the higher binding affinity of

Titration of the photocleavable cyclic peptide (cyclic-1) and the linear peptide resulting from light irradiation of cyclic-1 (photo-irradiated cyclic-1) into 15 N- labelled

Including these residues in a peptide increases the binding affinity around 30-fold compared to a peptide only containing the core binding motif, showing that residues outside

Given the fact that the flanking residues are mostly negatively charged, whereas the binding face of the SH2 domain contains many positively charged residues, the increase in

In tegenstelling tot wat werd verwacht voor een complex van hoge affiniteit, is met PRE NMR studies met spin- gelabelde peptiden vastgesteld dat de interactie tussen het peptide

[254] Xu RX, Word JM, Davis DG, Rink MJ, Willard DH, & Gampe RT (1995) Solution structure of the human pp60(C-Src) SH2 domain complexed with a phosphorylated

After having completed additional courses in molecular and cellular biology at Uppsala University, in May 2004 Hanna joined the medicinal chemistry group at the Leiden

Peripheral blood cells were stained with HLA-A2.1 tetramers containing the tyrosinase368–376 peptide followed by staining with a panel of lineage antibodies, as described in