23 research outputs found
The isolated N terminus of Ring1B is a well-folded, monomeric fragment with native-like structure
Accurate characterization of weak macromolecular interactions by titration of NMR residual dipolar couplings: application to the CD2AP SH3-C:ubiquitin complex
Structure, Function and Inhibition of the Phosphoethanolamine Methyltransferases of the Human Malaria Parasites Plasmodium vivax and Plasmodium knowlesi
Structural Model of the hUbA1-UbcH10 Quaternary Complex: In Silico and Experimental Analysis of the Protein-Protein Interactions between E1, E2 and Ubiquitin
Polycomb Protein SCML2 Associates with USP7 and Counteracts Histone H2A Ubiquitination in the XY Chromatin during Male Meiosis
NMR Spectroscopy in the Analysis of Protein-Protein Interactions
Protein-protein interactions are a central aspect of biology and NMR spectroscopyis one of the most powerful and versatile methods available to characterizetheir structure, dynamics, kinetics and thermodynamics. In this article, we give anoverview of the suite of approaches available to the researcher who wishes tounderstand their favourite protein-protein interaction in more detail. We beginwith an outline of two fundamental concepts that are important for understandingthe strengths and limitations of NMR spectroscopy – nuclear spin relaxation andchemical exchange. We then present a range of methods including chemical shiftperturbation analysis, nuclear Overhauser effects (and its derivatives), residualdipolar couplings, paramagnetic approaches, solid-state NMR and the analysis oflow-abundance species. Each method is accompanied by recen texamples fromthe literature. Together, these techniques can allow both broad and deep insightinto the mechanistic underpinnings of protein-protein interactions