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Updated: May 9, 2026

Nuclear Magnetic Resonance Spectroscopy for the Identification of Multiple Phosphorylations of Intrinsically Disordered Proteins
Published on: December 27, 2016
X-ray crystallography and NMR as tools for the study of protein tyrosine phosphatases
Irina Elena Gulerez1, Kalle Gehring1
1Department of Biochemistry and Groupe de recherche axé sur la structure des protéines, McGill University, 3649 Promenade Sir-William-Osler, Montreal, QC H3G 0B1, Canada.
Abstract:
Protein tyrosine phosphatases (PTPs) are well recognized as key targets in a wide spectrum of diseases, such as diabetes, obesity and cancer. Their roles in these maladies have been successfully characterized by various methods. However, it is only by utilizing the entire gamut of tools and techniques available that we can build a sufficient knowledge of their mode of action to bridge the gap between bench work and bedside treatments. Here, we highlight X-ray crystallography and NMR for the study of PTPs and describe methodological aspects of their use. These techniques are highly developed, versatile methods that together afford insight into protein dynamics, function and three-dimensional structure. They provide the detail necessary for the structure-based design and identification of lead compounds with potential as PTP-specific drugs for therapeutic use.
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