[NMR paper] Solid state NMR: The essential technology for helical membrane protein structural characterization.
Solid state NMR: The essential technology for helical membrane protein structural characterization.
Related Articles Solid state NMR: The essential technology for helical membrane protein structural characterization.
J Magn Reson. 2013 Dec 19;
Authors: Cross TA, Ekanayake V, Paulino J, Wright A
Abstract
NMR spectroscopy of helical membrane proteins has been very challenging on multiple fronts. The expression and purification of these proteins while maintaining functionality has consumed countless graduate student hours. Sample...
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01-15-2014 05:16 PM
[NMR paper] Solid State NMR Strategy for Characterizing Native Membrane Protein Structures.
Solid State NMR Strategy for Characterizing Native Membrane Protein Structures.
Related Articles Solid State NMR Strategy for Characterizing Native Membrane Protein Structures.
Acc Chem Res. 2013 Mar 7;
Authors: Murray DT, Das N, Cross TA
Abstract
Unlike water soluble proteins, the structures of helicaltransmembrane proteins depend on a very complex environment. These proteins sit in the midst of dramatic electrical and chemical gradients and are often subject to variations in the lateral pressure profile, order parameters, dielectric...
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03-09-2013 11:05 AM
Revealing Protein Structures in Solid-Phase Peptide Synthesis by 13C Solid-State NMR: Evidence of Excessive Misfolding for Alzheimer’s ?
Revealing Protein Structures in Solid-Phase Peptide Synthesis by 13C Solid-State NMR: Evidence of Excessive Misfolding for Alzheimer’s ?
Songlin Wang and Yoshitaka Ishii
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja212190z/aop/images/medium/ja-2011-12190z_0002.gif
Journal of the American Chemical Society
DOI: 10.1021/ja212190z
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/6EE7uthrnLg
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Characterization of different water pools in solid-state NMR protein samples
Characterization of different water pools in solid-state NMR protein samples
Abstract We observed and characterized two distinct signals originating from different pools of water protons in solid-state NMR protein samples, namely from crystal water which exchanges polarization with the protein (on the NMR timescale) and is located in the protein-rich fraction at the periphery of the magic-angle spinning (MAS) sample container, and supernatant water located close to the axis of the sample container. The polarization transfer between the water and the protein can be probed by...
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01-09-2011 12:46 PM
[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] Preparation of protein nanocrystals and their characterization by solid state NMR.
Preparation of protein nanocrystals and their characterization by solid state NMR.
Related Articles Preparation of protein nanocrystals and their characterization by solid state NMR.
J Magn Reson. 2003 Nov;165(1):162-74
Authors: Martin RW, Zilm KW
Preparation of proteins in their crystalline state has been found to be important in producing stable therapeutic protein formulations, cross-linked enzyme crystals for application in industrial processes, generating novel porous media for separations, and of course in structure elucidation. Of these...
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[NMR paper] Characterization of covalent protein conjugates using solid-state 13C NMR spectroscop
Characterization of covalent protein conjugates using solid-state 13C NMR spectroscopy.
Related Articles Characterization of covalent protein conjugates using solid-state 13C NMR spectroscopy.
Biochemistry. 1991 Jul 23;30(29):7057-62
Authors: Garbow JR, Fujiwara H, Sharp CR, Logusch EW
Cross-polarization magic-angle spinning (CPMAS) 13C NMR spectroscopy has been used to characterize covalent conjugates of alachlor, an alpha-chloroacetamide hapten, with glutathione (GSH) and bovine serum albumin (BSA). The solid-state NMR method demonstrates...
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08-21-2010 11:12 PM
[NMR paper] Characterization of covalent protein conjugates using solid-state 13C NMR spectroscop
Characterization of covalent protein conjugates using solid-state 13C NMR spectroscopy.
Related Articles Characterization of covalent protein conjugates using solid-state 13C NMR spectroscopy.
Biochemistry. 1991 Jul 23;30(29):7057-62
Authors: Garbow JR, Fujiwara H, Sharp CR, Logusch EW
Cross-polarization magic-angle spinning (CPMAS) 13C NMR spectroscopy has been used to characterize covalent conjugates of alachlor, an alpha-chloroacetamide hapten, with glutathione (GSH) and bovine serum albumin (BSA). The solid-state NMR method demonstrates...