Protein-protein interaction site mapping using NMR-detected mutational scanning.
|Abstract||We demonstrate a novel NMR method for the mapping of protein-protein interaction sites. In our approach protein-protein binding sites are mapped by competition binding experiments using indirect NMR reporter technology and Ala positional scanning. The methodology provides high sensitivity, ease of implementation and high-throughput capabilities. The feasibility of the technique is demonstrated with an application to the beta-Catenin/Tcf4 complex.|
|Author||Baminger, Bettina; Ludwiczek, Martin L; Kontaxis, Georg; et al|
|Subject||Binding, Competitive Humans Ligands Models, Molecular Mutation Nuclear Magnetic Resonance, Biomolecular Protein Interaction Mapping Reproducibility of Results TCF Transcription Factors Transcription Factor 7-Like 2 Protein beta Catenin genetics methods methods metabolism metabolism|
A homogeneous method for investigation of methylation-dependent protein-protein interactions in epigenetics.
|Abstract||Methylation of lysine residues on the tails of histone proteins is a major determinant of the transcription state of associated DNA coding regions. The interplay among methylation states and other histone modifications to direct transcriptional outcome is referred to as the histone code. In addition to histone methyltransferases and demethylases which function to modify the methylation state of lysine sidechains, other proteins recognize specific ... [truncated at 450 characters in length]|
|Author||Quinn, Amy M; Bedford, Mark T; Espejo, Alexsandra; et al|
|Subject||Binding, Competitive Chemiluminescent Measurements Chromosomal Proteins, Non-Histone Epigenesis, Genetic Histones Lysine Methylation Peptides Phosphoproteins Protein Interaction Domains and Motifs Protein Interaction Mapping chemistry metabolism chemistry metabolism metabolism metabolism chemistry metabolism methods|