Publication date: Available online 27 July 2013 Source:Methods
Author(s): Irina Elena Gulerez , Kalle Gehring
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.
[NMR paper] An overview of tools for the validation of protein NMR structures.
An overview of tools for the validation of protein NMR structures.
An overview of tools for the validation of protein NMR structures.
J Biomol NMR. 2013 Jul 23;
Authors: Vuister GW, Fogh RH, Hendrickx PM, Doreleijers JF, Gutmanas A
Abstract
Biomolecular structures at atomic resolution present a valuable resource for the understanding of biology. NMR spectroscopy accounts for 11*% of all structures in the PDB repository. In response to serious problems with the accuracy of some of the NMR-derived structures and in order to facilitate...
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[NMR paper] (13)C-(1)H NMR relaxation and fluorescence anisotropy decay study of tyrosine dynamic
(13)C-(1)H NMR relaxation and fluorescence anisotropy decay study of tyrosine dynamics in motilin.
Related Articles (13)C-(1)H NMR relaxation and fluorescence anisotropy decay study of tyrosine dynamics in motilin.
Biophys J. 2002 Nov;83(5):2812-25
Authors: Damberg P, Jarvet J, Allard P, Mets U, Rigler R, Gräslund A
Tyrosine ring dynamics of the gastrointestinal hormone motilin was studied using two independent physical methods: fluorescence polarization anisotropy decay and NMR relaxation. Motilin, a 22-residue peptide, was selectively (13)C...
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[NMR paper] Novel NMR tools to study structure and dynamics of biomembranes.
Novel NMR tools to study structure and dynamics of biomembranes.
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Chem Phys Lipids. 2002 Jun;116(1-2):135-51
Authors: Gawrisch K, Eldho NV, Polozov IV
Nuclear magnetic resonance (NMR) studies on biomembranes have benefited greatly from introduction of magic angle spinning (MAS) NMR techniques. Improvements in MAS probe technology, combined with the higher magnetic field strength of modern instruments, enables almost liquid-like resolution of lipid resonances. The...
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[NMR paper] Tools for the automated assignment of high-resolution three-dimensional protein NMR s
Tools for the automated assignment of high-resolution three-dimensional protein NMR spectra based on pattern recognition techniques.
Tools for the automated assignment of high-resolution three-dimensional protein NMR spectra based on pattern recognition techniques.
J Biomol NMR. 1997 Oct;10(3):207-19
Authors: Croft D, Kemmink J, Neidig KP, Oschkinat H
One of the major bottlenecks in the determination of proteinstructures by NMR is in the evaluation of the data produced by theexperiments. An important step in this process is assignment, where...
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[NMR paper] Tubulin-tyrosine ligase catalyzes covalent binding of 3-fluoro-tyrosine to tubulin: k
Tubulin-tyrosine ligase catalyzes covalent binding of 3-fluoro-tyrosine to tubulin: kinetic and NMR studies.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Tubulin-tyrosine ligase catalyzes covalent binding of 3-fluoro-tyrosine to tubulin: kinetic and NMR studies.
FEBS Lett. 1995 Oct 30;374(2):165-8
Authors: Monasterio O, Nova E, López-Brauet A, Lagos R
The use of 3-fluoro-tyrosine as an alternative substrate for the enzyme tubulin:tyrosine ligase which catalyzes the...
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08-22-2010 03:50 AM
[NMR paper] Solid-state 13C NMR study of tyrosine protonation in dark-adapted bacteriorhodopsin.
Solid-state 13C NMR study of tyrosine protonation in dark-adapted bacteriorhodopsin.
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Biochemistry. 1990 Jun 12;29(23):5567-74
Authors: Herzfeld J, Das Gupta SK, Farrar MR, Harbison GS, McDermott AE, Pelletier SL, Raleigh DP, Smith SO, Winkel C, Lugtenburg J
Solid-state 13C MAS NMR spectra were obtained for dark-adapted bacteriorhodopsin (bR) labeled with Tyr. Difference spectra (labeled minus natural abundance) taken at pH values between 2 and...
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A Solid-State (17)O NMR Study of l-Tyrosine in Different Ionization States: Implicati
A Solid-State (17)O NMR Study of l-Tyrosine in Different Ionization States: Implications for Probing Tyrosine Side Chains in Proteins.
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J Phys Chem B. 2010 Aug 16;
Authors: Zhu J, Lau JY, Wu G
We report experimental characterization of (17)O quadrupole coupling (QC) and chemical shift (CS) tensors for the phenolic oxygen in three l-tyrosine (l-Tyr) compounds: l-Tyr, l-Tyr.HCl, and Na(2)(l-Tyr)....
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Postdoctoral position to study Protein-Protein Interactions and their role in Mechanisms of Signal Transduction using protein solution NMR/x-ray crystallography
Spincore.com are advertising a postdoc NMR position. It sounds pretty interesting.
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Postdoctoral position to study Protein-Protein Interactions and their role in Mechanisms of Signal Transduction using protein solution NMR /x-ray crystallography
Case Medical School, Cleveland, Ohio, USA
How are signaling events transmitted from one protein to another? To answer this question we are looking to add a postdoctoral co-workers to our interdisciplinary team. Our interest is to understand protein-protein interactions, protein structure and dynamics in the context of cell signaling...
X-ray crystallography and NMR as tools for the study of protein tyrosine phosphatases
Linear Mode
