Related ArticlesHigh-resolution solid-state NMR studies on uniformly [13C,15N]-labeled ubiquitin.
Chembiochem. 2005 Sep;6(9):1638-47
Authors: Seidel K, Etzkorn M, Heise H, Becker S, Baldus M
Understanding of the effects of intermolecular interactions, molecular dynamics, and sample preparation on high-resolution magic-angle spinning NMR data is currently limited. Using the example of a uniformly [13C,15N]-labeled sample of ubiquitin, we discuss solid-state NMR methods tailored to the construction of 3D molecular structure and study the influence of solid-phase protein preparation on solid-state NMR spectra. A comparative analysis of 13C', 13Calpha, and 13Cbeta resonance frequencies suggests that 13C chemical-shift variations are most likely to occur in protein regions that exhibit an enhanced degree of molecular mobility. Our results can be refined by additional solid-state NMR techniques and serve as a reference for ongoing efforts to characterize the structure and dynamics of (membrane) proteins, protein complexes, and other biomolecules by high-resolution solid-state NMR.
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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10-10-2011 06:27 AM
Uniform isotope labeling of a eukaryotic seven-transmembrane helical protein in yeast enables high-resolution solid-state NMR studies in the lipid environment
Uniform isotope labeling of a eukaryotic seven-transmembrane helical protein in yeast enables high-resolution solid-state NMR studies in the lipid environment
Abstract Overexpression of isotope-labeled multi-spanning eukaryotic membrane proteins for structural NMR studies is often challenging. On the one hand, difficulties with achieving proper folding, membrane insertion, and native-like post-translational modifications frequently disqualify bacterial expression systems. On the other hand, eukaryotic cell cultures can be prohibitively expensive. One of the viable alternatives,...
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01-22-2011 03:46 AM
Uniform isotope labeling of a eukaryotic seven-transmembrane helical protein in yeast enables high-resolution solid-state NMR studies in the lipid environment.
Uniform isotope labeling of a eukaryotic seven-transmembrane helical protein in yeast enables high-resolution solid-state NMR studies in the lipid environment.
Uniform isotope labeling of a eukaryotic seven-transmembrane helical protein in yeast enables high-resolution solid-state NMR studies in the lipid environment.
J Biomol NMR. 2011 Jan 19;
Authors: Fan Y, Shi L, Ladizhansky V, Brown LS
Overexpression of isotope-labeled multi-spanning eukaryotic membrane proteins for structural NMR studies is often challenging. On the one hand, difficulties...
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01-21-2011 01:22 AM
[NMR paper] High-resolution solid-state NMR spectroscopy of the prion protein HET-s in its amyloi
High-resolution solid-state NMR spectroscopy of the prion protein HET-s in its amyloid conformation.
Related Articles High-resolution solid-state NMR spectroscopy of the prion protein HET-s in its amyloid conformation.
Angew Chem Int Ed Engl. 2005 Apr 15;44(16):2441-4
Authors: Siemer AB, Ritter C, Ernst M, Riek R, Meier BH
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11-25-2010 08:21 PM
[NMR paper] Towards high-resolution solid-state NMR on large uniformly 15N- and [13C,15N]-labeled
Towards high-resolution solid-state NMR on large uniformly 15N- and -labeled membrane proteins in oriented lipid bilayers.
Related Articles Towards high-resolution solid-state NMR on large uniformly 15N- and -labeled membrane proteins in oriented lipid bilayers.
J Biomol NMR. 2002 Mar;22(3):225-47
Authors: Vosegaard T, Nielsen NC
Based on exact numerical simulations, taking into account isotropic and conformation-dependent anisotropic nuclear spin interactions, we systematically analyse the prospects for high-resolution solid-state NMR on...
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11-24-2010 08:49 PM
High resolution 13C-detected solid-state NMR spectroscopy of a deuterated protein
High resolution 13C-detected solid-state NMR spectroscopy of a deuterated protein
Abstract High resolution 13C-detected solid-state NMR spectra of the deuterated beta-1 immunoglobulin binding domain of the protein G (GB1) have been collected to show that all 15N, 13Cā?², 13CĪ± and 13CĪ² sites are resolved in 13Cā??13C and 15Nā??13C spectra, with significant improvement in T 2 relaxation times and resolution at high magnetic field (750 MHz). The comparison of echo T 2 values between deuterated and protonated GB1 at various spinning rates and under different decoupling schemes indicates...
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09-01-2010 10:56 AM
[NMR paper] Complete resolution of the solid-state NMR spectrum of a uniformly 15N-labeled membra
Complete resolution of the solid-state NMR spectrum of a uniformly 15N-labeled membrane protein in phospholipid bilayers.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--highwire.stanford.edu-icons-externalservices-pubmed-custom-pnas_full_free.gif http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles Complete resolution of the solid-state NMR spectrum of a uniformly 15N-labeled membrane protein in phospholipid bilayers.
Proc Natl Acad Sci U S A. 1997 Aug 5;94(16):8551-6
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08-22-2010 05:08 PM
[NMR paper] High-level expression of uniformly 15N-labeled hen lysozyme in Pichia pastoris and id
High-level expression of uniformly 15N-labeled hen lysozyme in Pichia pastoris and identification of the site in hen lysozyme where phosphate ion binds using NMR measurements.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles High-level expression of uniformly 15N-labeled hen lysozyme in Pichia pastoris and identification of the site in hen lysozyme where phosphate ion binds using NMR measurements.
FEBS Lett. 1999 Apr 1;448(1):33-7
Authors: Mine S, Ueda T, Hashimoto Y, Tanaka Y,...
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High-resolution solid-state NMR studies on uniformly [13C,15N]-labeled ubiquitin.
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