[NMR paper] Characterization of protein-ligand interactions by high-resolution solid-state NMR sp
Characterization of protein-ligand interactions by high-resolution solid-state NMR spectroscopy.
Related Articles Characterization of protein-ligand interactions by high-resolution solid-state NMR spectroscopy.
J Am Chem Soc. 2004 Nov 3;126(43):13948-53
Authors: Zech SG, Olejniczak E, Hajduk P, Mack J, McDermott AE
A novel approach for detection of ligand binding to a protein in solid samples is described. Hydrated precipitates of the anti-apoptotic protein Bcl-xL show well-resolved (13)C-(13)C 2D solid-state NMR spectra that allow...
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11-24-2010 10:03 PM
[NMR paper] Selective observation of the Cu(I)-amicyanin metal site by paramagnetic NMR on partia
Selective observation of the Cu(I)-amicyanin metal site by paramagnetic NMR on partially oxidised samples.
Selective observation of the Cu(I)-amicyanin metal site by paramagnetic NMR on partially oxidised samples.
J Biomol NMR. 1997 Apr;9(3):299-305
Authors: Salgado J, Kalverda AP, Canters GW
The relaxation enhancement caused by paramagnetic copper(II) is used to observe selectivelythe metal site of copper(I)-amicyanin by one- and two-dimensional NMR spectroscopy. Theparamagnetic effect is communicated to the diamagnetic protein through the...
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08-22-2010 03:31 PM
[NMR paper] Selective observation of the Cu(I)-amicyanin metal site by paramagnetic NMR on partia
Selective observation of the Cu(I)-amicyanin metal site by paramagnetic NMR on partially oxidised samples.
Selective observation of the Cu(I)-amicyanin metal site by paramagnetic NMR on partially oxidised samples.
J Biomol NMR. 1997 Apr;9(3):299-305
Authors: Salgado J, Kalverda AP, Canters GW
The relaxation enhancement caused by paramagnetic copper(II) is used to observe selectivelythe metal site of copper(I)-amicyanin by one- and two-dimensional NMR spectroscopy. Theparamagnetic effect is communicated to the diamagnetic protein through the...
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08-22-2010 03:03 PM
[NMR paper] Selective and extensive 13C labeling of a membrane protein for solid-state NMR invest
Selective and extensive 13C labeling of a membrane protein for solid-state NMR investigations.
Related Articles Selective and extensive 13C labeling of a membrane protein for solid-state NMR investigations.
J Biomol NMR. 1999 May;14(1):71-4
Authors: Hong M, Jakes K
The selective and extensive 13C labeling of mostly hydrophobic amino acid residues in a 25 kDa membrane protein, the colicin Ia channel domain, is reported. The novel 13C labeling approach takes advantage of the amino acid biosynthetic pathways in bacteria and suppresses the...
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08-21-2010 04:03 PM
Solid-State (17)O NMR Spectroscopy of Large Protein-Ligand Complexes.
Solid-State (17)O NMR Spectroscopy of Large Protein-Ligand Complexes.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_120x27.gif Related Articles Solid-State (17)O NMR Spectroscopy of Large Protein-Ligand Complexes.
Angew Chem Int Ed Engl. 2010 Jul 29;
Authors: Zhu J, Ye E, Terskikh V, Wu G
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08-17-2010 03:36 AM
Solid-State (17)O NMR Spectroscopy of Large Protein-Ligand Complexes.
Solid-State (17)O NMR Spectroscopy of Large Protein-Ligand Complexes.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_120x27.gif Related Articles Solid-State (17)O NMR Spectroscopy of Large Protein-Ligand Complexes.
Angew Chem Int Ed Engl. 2010 Jul 28;
Authors: Zhu J, Ye E, Terskikh V, Wu G
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High Resolution 1H Detected 1H,13C Correlation Spectra in MAS Solid-State NMR using Deuterated Proteins with Selective 1H,2H Isotopic Labeling of Methyl Groups
High Resolution <SUP>1</SUP>H Detected <SUP>1</SUP>H,<SUP>13</SUP>C Correlation Spectra in MAS Solid-State NMR using Deuterated Proteins with Selective <SUP>1</SUP>H,<SUP>2</SUP>H Isotopic Labeling of Methyl Groups
Vipin Agarwal, Anne Diehl, Nikolai Skrynnikov, and Bernd Reif
J. Am. Chem. Soc.; 2006; 128(39) pp 12620 - 12621;
Abstract:
MAS solid-state NMR experiments applied to biological solids are still hampered by low sensitivity and resolution. In this work, we employ a deuteration scheme in which individual methyl groups are selectively protonated. This labeling scheme...
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08-05-2009 03:21 AM
Ligand-membrane protein binding by solid-state NMR
Selective Interface Detection: Mapping Binding Site Contacts in Membrane Proteins by NMR Spectroscopy
Suzanne R. Kiihne, Alain F. L. Creemers, Willem J. de Grip, Petra H. M. Bovee-Geurts, Johan Lugtenburg, and Huub J. M. de Groot
J. Am. Chem. Soc.; 2005; 127(16) pp 5734 - 5735
ABSTRACT:
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...