Measurement of dissociation constants of inhibitors binding to Src SH2 domain protein by non-covalent electrospray ionization mass spectrometry
Author:
Publisher
Wiley
Subject
Molecular Biology,Structural Biology
Reference21 articles.
1. Probing the “Two-Pronged Plug Two-Holed Socket” Model for the Mechanism of Binding of the Src SH2 Domain to Phosphotyrosyl Peptides: A Thermodynamic Study
2. Mass spectrometric and thermodynamic studies reveal the role of water molecules in complexes formed between SH2 domains and tyrosyl phosphopeptides
3. Probing the nature of interactions in SH2 binding interfaces-evidence from electrospray ionization mass spectrometry
4. Peptide inhibitors of src SH3-SH2-phosphoprotein interactions.
5. Measurement of Macromolecular Binding Using Electrospray Mass Spectrometry. Determination of Dissociation Constants for Oligonucleotide: Serum Albumin Complexes
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