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NMR spectroscopy has a unique ability to describe concurrent molecular events, such as phosphorylation, which cannot be characterized individually by other methods. By combining heteronuclear NMR methods and selective protein… Click to show full abstract
NMR spectroscopy has a unique ability to describe concurrent molecular events, such as phosphorylation, which cannot be characterized individually by other methods. By combining heteronuclear NMR methods and selective protein labelling we aim to build a quantitative approach for the analysis of multi-site phosphorylation and related structural changes in proteins. Particularly, we are studying kinetics of phosphorylation, order of the phosphorylation events, and related structural changes within immunoreceptor tyrosine-based activation motifs (ITAM) at the mostly unstructured cytosolic domains of signal-propagating CD3 subunits of T-cell receptor (TCR) complex.
Journal Title: Biophysical Journal
Year Published: 2017
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