Related ArticlesMultidimensional NMR spectroscopy for protein characterization and assignment inside cells.
J Am Chem Soc. 2005 Aug 10;127(31):10848-9
Authors: Reardon PN, Spicer LD
High-field, heteronuclear NMR spectroscopy of biological macromolecules in native cellular environments is limited by the low concentrations present and the long data acquisition times needed for the experiments. Successful 1D and 2D heteronuclear NMR data have been reported, but the 3D experiments conventionally used for protein assignment and detailed characterization are generally too long to maintain cell viability. Here we describe the successful in vivo implementation of a suite of fast 3D NMR experiments which we have used to generate the complete backbone assignment of resonances in the recombinant polypeptide GB-1 within Escherichia coli cells. The data were acquired at 600 MHz with a cold probe using the projection reconstruction experiments, (3,2)HNCA, (3,2)HNCO, and (3,2)HA(CA)NH.
Multidimensional oriented solid-state NMR experiments enable the sequential assignment of uniformly 15N labeled integral membrane proteins in magnetically aligned lipid bilayers
Multidimensional oriented solid-state NMR experiments enable the sequential assignment of uniformly 15N labeled integral membrane proteins in magnetically aligned lipid bilayers
Abstract Oriented solid-state NMR is the most direct methodology to obtain the orientation of membrane proteins with respect to the lipid bilayer. The method consists of measuring 1H-15N dipolar couplings (DC) and 15N anisotropic chemical shifts (CSA) for membrane proteins that are uniformly aligned with respect to the membrane bilayer. A significant advantage of this approach is that tilt and azimuthal...
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13C direct-detection biomolecular NMR spectroscopy in living cells.
13C direct-detection biomolecular NMR spectroscopy in living cells.
13C direct-detection biomolecular NMR spectroscopy in living cells.
Angew Chem Int Ed Engl. 2011 Mar 1;50(10):2339-41
Authors: Bertini I, Felli IC, Gonnelli L, Kumar M V V, Pierattelli R
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[NMR paper] Dynamics of xenon binding inside the hydrophobic cavity of pseudo-wild-type bacteriophage T4 lysozyme explored through xenon-based NMR spectroscopy.
Dynamics of xenon binding inside the hydrophobic cavity of pseudo-wild-type bacteriophage T4 lysozyme explored through xenon-based NMR spectroscopy.
Related Articles Dynamics of xenon binding inside the hydrophobic cavity of pseudo-wild-type bacteriophage T4 lysozyme explored through xenon-based NMR spectroscopy.
J Am Chem Soc. 2005 Aug 24;127(33):11676-83
Authors: Desvaux H, Dubois L, Huber G, Quillin ML, Berthault P, Matthews BW
Wild-type bacteriophage T4 lysozyme contains a hydrophobic cavity with binding properties that have been...
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12-01-2010 06:56 PM
[NMR paper] NMR assignment and structural characterization of the fatty acid binding protein from
NMR assignment and structural characterization of the fatty acid binding protein from the flight muscle of Locusta migratoria.
Related Articles NMR assignment and structural characterization of the fatty acid binding protein from the flight muscle of Locusta migratoria.
J Biomol NMR. 2003 Apr;25(4):355-6
Authors: Lücke C, Kizilbash N, van Moerkerk HT, Veerkamp JH, Hamilton JA
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[NMR paper] Graph-theoretical assignment of secondary structure in multidimensional protein NMR s
Graph-theoretical assignment of secondary structure in multidimensional protein NMR spectra: application to the lac repressor headpiece.
Related Articles Graph-theoretical assignment of secondary structure in multidimensional protein NMR spectra: application to the lac repressor headpiece.
J Biomol NMR. 1995 Jul;6(1):67-78
Authors: van Geerestein-Ujah EC, Slijper M, Boelens R, Kaptein R
A novel procedure is presented for the automatic identification of secondary structures in proteins from their corresponding NOE data. The method uses a branch...
Multidimensional NMR spectroscopy for protein characterization and assignment inside cells.
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