Related Articles(15)N and (13)C Group-Selective Techniques Extend the Scope of STD NMR Detection of Weak Host-Guest Interactions and Ligand Screening.
Chembiochem. 2010 Sep 28;
Authors: Kövér KE, Wéber E, Martinek TA, Monostori E, Batta G
Saturation transfer difference (STD) is a valuable tool for studying the binding of small molecules to large biomolecules and for obtaining detailed information on the binding epitopes. Here, we demonstrate that the proposed (15)N/(13)C variants of group-selective, "GS-STD" experiments provide a powerful approach to mapping the binding epitope of a ligand even in the absence of efficient spin diffusion within the target protein. Therefore, these experimental variants broaden the scope of STD studies to smaller and/or more-dynamic targets. The STD spectra obtained in four different experimental setups (selective (1)H STD, (15)N GS-STD, (13)C(Ar) and (13)C(aliphatic) GS-STD approaches) revealed that the signal-intensity pattern of the difference spectra is affected by both the type and the spatial distribution of the excited "transmitter" atoms, as well as by the efficiency of the spin-diffusion-mediated magnetization transfer. The performance of the experiments is demonstrated on a system by using the lectin, galectin-1 and its carbohydrate ligand, lactose.
PMID: 20878964 [PubMed - as supplied by publisher]
Generative probabilistic models extend the scope of inferential structure determination
Generative probabilistic models extend the scope of inferential structure determination
Publication year: 2011
Source: Journal of Magnetic Resonance, In Press, Accepted Manuscript, Available online 6 September 2011</br>
Simon, Olsson , Wouter, Boomsma , Jes, Frellsen , Sandro, Bottaro , Tim, Harder , ...</br>
Conventional methods for protein structure determination from NMR data rely on the ad hoc combination of physical forcefields and experimental data, along with heuristic determination of free parameters such as weight of experimental data relative to a physical forcefield....
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Frequency-selective heteronuclear dephasing and selective carbonyl labeling to deconvolute crowded spectra of membrane proteins by magic angle spinning NMR.
Frequency-selective heteronuclear dephasing and selective carbonyl labeling to deconvolute crowded spectra of membrane proteins by magic angle spinning NMR.
Frequency-selective heteronuclear dephasing and selective carbonyl labeling to deconvolute crowded spectra of membrane proteins by magic angle spinning NMR.
J Magn Reson. 2011 Mar 17;
Authors: Traaseth NJ, Veglia G
We present a new method that combines carbonyl-selective labeling with frequency-selective heteronuclear recoupling to resolve the spectral overlap of magic angle spinning (MAS) NMR...
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Frequency-Selective Heteronuclear Dephasing and Selective Carbonyl Labeling to Deconvolute Crowded Spectra of Membrane Proteins By Magic Angle Spinning NMR
Frequency-Selective Heteronuclear Dephasing and Selective Carbonyl Labeling to Deconvolute Crowded Spectra of Membrane Proteins By Magic Angle Spinning NMR
Publication year: 2011
Source: Journal of Magnetic Resonance, In Press, Accepted Manuscript, Available online 17 March 2011</br>
Nathaniel J., Traaseth , Gianluigi, Veglia</br>
We present a new method that combines carbonyl-selective labeling with frequency-selective heteronuclear recoupling to resolve the spectral overlap of magic angle spinning (MAS) NMR spectra of membrane proteins in fluid lipid membranes with broad lines and...
Selective Detection of 13CHD2 Signals from a Mixture of 13CH3/13CH2D/13CHD2 Methyl Isotopomers in Proteins
Selective Detection of 13CHD2 Signals from a Mixture of 13CH3/13CH2D/13CHD2 Methyl Isotopomers in Proteins
Publication year: 2011
Source: Journal of Magnetic Resonance, In Press, Accepted Manuscript, Available online 4 January 2011</br>
Xinli, Liao , Vitali, Tugarinov</br>
In NMR spectra of partially deuterated proteins methyl correlations are commonly observed as a combination of signals from 13CH3, 13CH2D and 13CHD2 isotopomers. In a number of NMR applications, methyl groups of the 13CHD2 variety are targeted because of their AX-like character and concomitant simplification of the...
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[NMR paper] Selective interface detection: mapping binding site contacts in membrane proteins by
Selective interface detection: mapping binding site contacts in membrane proteins by NMR spectroscopy.
Related Articles Selective interface detection: mapping binding site contacts in membrane proteins by NMR spectroscopy.
J Am Chem Soc. 2005 Apr 27;127(16):5734-5
Authors: Kiihne SR, Creemers AF, de Grip WJ, Bovee-Geurts PH, Lugtenburg J, de Groot HJ
Intermolecular contact surfaces are important regions where specific interactions mediate biological function. We introduce a new magic angle spinning solid state NMR technique, dubbed "selective...
[NMR paper] Expanding the Scope of Protein Biosynthesis by Altering the Methionyl-tRNA Synthetase
Expanding the Scope of Protein Biosynthesis by Altering the Methionyl-tRNA Synthetase Activity of a Bacterial Expression Host Scott Ross was helpful in conducting the 1D TOCSY NMR experiments and Pratip Bhattachary is thanked for assistance in other NMR experiments. We are grateful to Yves Mechulam for a sample of plasmid pBSM547W305F and to Hieronim Jakubowski of UMDNJ-New Jersey Medical School, Newark, New Jersey, for plasmid pGG3. K.L.K. thanks the U.S. Department of Defense for a National Defense Science and Engineering Graduate Fellowship. This work was supported by grants from the...
(15)N and (13)C Group-Selective Techniques Extend the Scope of STD NMR Detection of W
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