Related ArticlesSelective 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 interface detection spectroscopy" (SIDY). In this technique, 13C-attached protons (1Hlig) are dephased by 1H-13C REDOR. A spin diffusion period is then used to enhance long distance 1H-1H correlations, and the results are detected by a short period of cross polarization to the 13C isotope labels. This SIDY approach allows selective observation of the interface between 13C-labeled and unlabeled moieties. We have used SIDY to probe the ligand-protein binding surface between a uniformly isotopically labeled ligand cofactor, U-13C20-11-cis-retinal, and its binding site in rhodopsin (Rho), an unlabeled, membrane-embedded G-protein coupled receptor (GPCR). The observed 1HGPCR-13Clig correlations indicate multiple close contacts between the protein and the ionone ring of the ligand, in agreement with binding studies. The polyene tail of the ligand displays fewer strong correlations in the SIDY spectrum. Some correlations can be assigned to the protein side chains lining the ligand binding site, in agreement with the crystal structure.
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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04-13-2011 11:57 PM
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...
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03-18-2011 06:43 AM
[NMR paper] Mapping the binding site of full length HIV-1 Nef on human Lck SH3 by NMR spectroscop
Mapping the binding site of full length HIV-1 Nef on human Lck SH3 by NMR spectroscopy.
Related Articles Mapping the binding site of full length HIV-1 Nef on human Lck SH3 by NMR spectroscopy.
J Biomed Sci. 2005;12(3):451-6
Authors: Briese L, Preusser A, Willbold D
The Nef protein of human immunodeficiency virus type 1 (HIV-1) is known to directly bind to the SH3 domain of human lymphocyte specific kinase (Lck) via a proline-rich region located in the amino terminal part of Nef. To address the question whether Nef binding to Lck SH3 involves...
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11-24-2010 11:14 PM
[NMR paper] Biochemical and NMR mapping of the interface between CREB-binding protein and ligand
Biochemical and NMR mapping of the interface between CREB-binding protein and ligand binding domains of nuclear receptor: beyond the LXXLL motif.
Related Articles Biochemical and NMR mapping of the interface between CREB-binding protein and ligand binding domains of nuclear receptor: beyond the LXXLL motif.
J Biol Chem. 2005 Feb 18;280(7):5682-92
Authors: Klein FA, Atkinson RA, Potier N, Moras D, Cavarelli J
CBP, cAMP-response element-binding protein (CREB)-binding protein, plays an important role as a general cointegrator of various signaling...
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11-24-2010 10:03 PM
[NMR paper] Epitope mapping and competitive binding of HSA drug site II ligands by NMR diffusion
Epitope mapping and competitive binding of HSA drug site II ligands by NMR diffusion measurements.
Related Articles Epitope mapping and competitive binding of HSA drug site II ligands by NMR diffusion measurements.
J Am Chem Soc. 2004 Nov 3;126(43):14258-66
Authors: Lucas LH, Price KE, Larive CK
It is important to characterize drug-albumin binding during drug discovery and lead optimization as strong binding may reduce bioavailability and/or increase the drug's in vivo half-life. Despite knowing about the location of human serum albumin (HSA)...
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11-24-2010 10:03 PM
[NMR paper] Ubiquitin binding interface mapping on yeast ubiquitin hydrolase by NMR chemical shif
Ubiquitin binding interface mapping on yeast ubiquitin hydrolase by NMR chemical shift perturbation.
Related Articles Ubiquitin binding interface mapping on yeast ubiquitin hydrolase by NMR chemical shift perturbation.
Biochemistry. 1999 Jul 20;38(29):9242-53
Authors: Rajesh S, Sakamoto T, Iwamoto-Sugai M, Shibata T, Kohno T, Ito Y
The interaction between the 26 kDa yeast ubiquitin hydrolase (YUH1), involved in maintaining the monomeric ubiquitin pool in cells, and the 8.5 kDa yeast ubiquitin protein has been studied by heteronuclear...
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11-18-2010 08:31 PM
Simultaneous detection of amide and methyl correlations using a time shared NMR experiment: application to binding epitope mapping
Simultaneous detection of amide and methyl correlations using a time shared NMR experiment: application to binding epitope mapping
Peter Würtz, Olli Aitio, Maarit Hellman and Perttu Permi
Journal of Biomolecular NMR; 2007; 39(2) pp 97 - 105
Abstract:
Simultaneous recording of different NMR parameters is an efficient way to reduce the overall experimental time and speed up structural studies of biological macromolecules. This can especially be beneficial in the case of fast NMR-based drug screening applications or for collecting NOE restraints, where prohibitively long data collection...