Practical considerations over spectral quality in solid state NMR spectroscopy of soluble proteins.
J Biomol NMR. 2013 Aug 30;
Authors: Fragai M, Luchinat C, Parigi G, Ravera E
Abstract
Great theoretical and methodological advances are pushing the limits of resolution and sensitivity in solid state NMR (SSNMR). However, sample preparation remains a critical issue for the success of an experiment. The factors affecting spectral quality in SSNMR samples are discussed, examining cases encountered in the literature and presenting new experimental data. A discussion on resolution and sensitivity in sedimented solutes is framed in this context.
PMID: 23990200 [PubMed - as supplied by publisher]
Solid-State NMR Spectroscopy of Proteins
From The DNP-NMR Blog:
Solid-State NMR Spectroscopy of Proteins
A nice review about solid-state NMR spectroscopy with some solid-state DNP.
Müller, H., M. Etzkorn, and H. Heise, Solid-State NMR Spectroscopy of Proteins, in Modern NMR Methodology, H. Heise and S. Matthews, Editors. 2013, Springer Berlin Heidelberg. p. 121-156.
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07-12-2013 06:01 PM
[NMR paper] Solid-State NMR Spectroscopy of Proteins.
Solid-State NMR Spectroscopy of Proteins.
Related Articles Solid-State NMR Spectroscopy of Proteins.
Top Curr Chem. 2013 Mar 16;
Authors: Müller H, Etzkorn M, Heise H
Abstract
Solid-state NMR spectroscopy proved to be a versatile tool for characterization of structure and dynamics of complex biochemical systems. In particular, magic angle spinning (MAS) solid-state NMR came to maturity for application towards structural elucidation of biological macromolecules. Current challenges in applying solid-state NMR as well as progress achieved...
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03-19-2013 01:22 PM
TROSY NMR Spectroscopy of Large Soluble Proteins.
TROSY NMR Spectroscopy of Large Soluble Proteins.
TROSY NMR Spectroscopy of Large Soluble Proteins.
Top Curr Chem. 2011 Sep 17;
Authors: Xu Y, Matthews S
Abstract
Solution nuclear magnetic resonance spectroscopy is usually only used to study proteins with molecular weight not exceeding about 50 kDa. This size limit has been lifted significantly in recent years, thanks to the development of labelling methods and the application of transverse-relaxation optimized spectroscopy (TROSY). In particular, methyl-specific labelling and...
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09-20-2011 03:10 PM
[NMR paper] 2D solid state NMR spectral simulation of 3(10), alpha, and pi-helices.
2D solid state NMR spectral simulation of 3(10), alpha, and pi-helices.
Related Articles 2D solid state NMR spectral simulation of 3(10), alpha, and pi-helices.
J Magn Reson. 2004 Jun;168(2):187-93
Authors: Kim S, Cross TA
Transmembrane helices are more uniform in structure than similar helices in water soluble proteins. Solid state NMR of aligned bilayer samples is being increasingly used to characterize helical membrane protein structures. Traditional spectroscopic methods have difficulty distinguishing between helices with i to i + 3...
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11-24-2010 09:51 PM
[NMR paper] Solid-state NMR investigation of the dynamics of the soluble and membrane-bound colic
Solid-state NMR investigation of the dynamics of the soluble and membrane-bound colicin Ia channel-forming domain.
Related Articles Solid-state NMR investigation of the dynamics of the soluble and membrane-bound colicin Ia channel-forming domain.
Biochemistry. 2001 Jun 26;40(25):7662-74
Authors: Huster D, Xiao L, Hong M
Solid-state NMR spectroscopy was employed to study the molecular dynamics of the colicin Ia channel domain in the soluble and membrane-bound states. In the soluble state, the protein executes small-amplitude librations (with...
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11-19-2010 08:32 PM
[NMR paper] Solid-state dipolar INADEQUATE NMR spectroscopy with a large double-quantum spectral
Solid-state dipolar INADEQUATE NMR spectroscopy with a large double-quantum spectral width.
Related Articles Solid-state dipolar INADEQUATE NMR spectroscopy with a large double-quantum spectral width.
J Magn Reson. 1999 Jan;136(1):86-91
Authors: Hong M
A technique for obtaining dipolar-mediated INADEQUATE NMR spectra with a large spectral window in the double-quantum dimension is presented. Using the dipolar recoupling sequence C7 to excite the double-quantum coherence under magic-angle spinning, the technique involves incrementing the...
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11-18-2010 07:05 PM
GFT projection NMR spectroscopy for proteins in the solid state.
GFT projection NMR spectroscopy for proteins in the solid state.
GFT projection NMR spectroscopy for proteins in the solid state.
J Biomol NMR. 2010 Oct 30;
Authors: Trent Franks W, Atreya HS, Szyperski T, Rienstra CM
Recording of four-dimensional (4D) spectra for proteins in the solid state has opened new avenues to obtain virtually complete resonance assignments and three-dimensional (3D) structures of proteins. As in solution state NMR, the sampling of three indirect dimensions leads per se to long minimal measurement time. Furthermore,...
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11-06-2010 11:02 AM
Protein alignment using cellulose nanocrystals: practical considerations and range of
Abstract Cellulose nanocrystals (CNCs) form liquid crystals in aqueous solution that confer alignment to macromolecules and permit the measurement of residual dipolar couplings. CNCs possess many attractive features as an alignment medium. They are inexpensive, non-toxic, chemically inert, and robust to denaturants and temperature. Despite these advantages, CNCs are seldom employed as an alignment medium and the range of their applicability has not yet been explored. We have re-examined the use of CNCs in biomolecular NMR by analyzing the effects concentration, ionic strength, and...
Practical considerations over spectral quality in solid state NMR spectroscopy of soluble proteins.
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