| Literature DB >> 27514807 |
Wolfgang Peti1,2, Rebecca Page3.
Abstract
NMR spectroscopy and other solution methods are increasingly being used to obtain novel insights into the mechanisms by which MAPK regulatory proteins bind and direct the activity of MAPKs. Here, we describe how interactions between the MAPK p38α and its regulatory proteins are studied using NMR spectroscopy, isothermal titration calorimetry, and small angle X-ray scattering (SAXS).Keywords: Chemical shift perturbation (CSP); D2O; Dual specificity phosphatase; Isothermal titration calorimetry (ITC); Isotopically labeled growth media; Mitogen activated protein kinase (MAPK); Nuclear magnetic resonance (NMR) spectroscopy; Protein tyrosine phosphatases; Protein–protein interaction; Small angle X-ray scattering (SAXS); p38α
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Year: 2016 PMID: 27514807 DOI: 10.1007/978-1-4939-3746-2_11
Source DB: PubMed Journal: Methods Mol Biol ISSN: 1064-3745