Related ArticlesHigh resolution 13C-solid state NMR of bacteriorhodopsin: assignment of specific aspartic acids and structural implications of single site mutations.
Eur Biophys J. 1990;18(1):17-24
Authors: Engelhard M, Hess B, Metz G, Kreutz W, Siebert F, Soppa J, Oesterhelt D
Three mutant strains of Halobacterium sp. GRB with the site of mutation in the bacterioopsin gene (PM 326: Asp96----Asn; PM 374: Asp96----Gly; PM 384: Asp85----Glu) were grown in a synthetic medium containing (4-13C)-Asp. The mutant bacteriorhodopsins labeled with (4-13C)-Asp (37%-45%), and owing to the metabolism of Halobacteria also with (11-13C)-Trp (50%-100%), were isolated as purple membranes and 13C Solid State Magic Angle Sample Spinning (MASS) Nuclear Magnetic Resonance (NMR) spectra of the samples were taken. The Asp96 mutants lacked the signal at 171.3 ppm which was previously assigned to a protonated internal Asp (Engelhard et al. 1989a). This observation supports the conclusion that Asp96 is protonated in the ground state. PM 384 (Asp85----Glu) has an absorption maximum at 610 nm. It can be converted into a purple form (lambda max = 540 nm) by treatment with a detergent (CHAPSO). The NMR-spectra of these two species differ from each other and from the wild type. The intensity of the resonance at 173 ppm in the wild type spectrum is reduced in both forms of the mutant protein. It is probable that this signal is caused by Asp85. The amino acid changes result not only in a perturbation of their direct environment but also effects on Trp residues and the chromophore protein interaction can be observed.
[NMR paper] High-resolution solid-state NMR studies on uniformly [13C,15N]-labeled ubiquitin.
High-resolution solid-state NMR studies on uniformly -labeled ubiquitin.
Related Articles High-resolution solid-state NMR studies on uniformly -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 -labeled sample of ubiquitin, we discuss solid-state NMR methods tailored to the...
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[NMR paper] Protein structure determination by high-resolution solid-state NMR spectroscopy: appl
Protein structure determination by high-resolution solid-state NMR spectroscopy: application to microcrystalline ubiquitin.
Related Articles Protein structure determination by high-resolution solid-state NMR spectroscopy: application to microcrystalline ubiquitin.
J Am Chem Soc. 2005 Jun 22;127(24):8618-26
Authors: Zech SG, Wand AJ, McDermott AE
High-resolution solid-state NMR spectroscopy has become a promising method for the determination of three-dimensional protein structures for systems which are difficult to crystallize or exhibit low...
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[NMR paper] Investigation of ligand-receptor systems by high-resolution solid-state NMR: recent p
Investigation of ligand-receptor systems by high-resolution solid-state NMR: recent progress and perspectives.
Related Articles Investigation of ligand-receptor systems by high-resolution solid-state NMR: recent progress and perspectives.
Arch Pharm (Weinheim). 2005 Jun;338(5-6):217-28
Authors: Luca S, Heise H, Lange A, Baldus M
Solid-state Nuclear Magnetic Resonance (NMR) provides a general method to study molecular structure and dynamics in a non-crystalline and insoluble environment. We discuss the latest methodological progress to...
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[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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[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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[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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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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High resolution (13)C-detected solid-state NMR spectroscopy of a deuterated protein.
High resolution (13)C-detected solid-state NMR spectroscopy of a deuterated protein.
Related Articles High resolution (13)C-detected solid-state NMR spectroscopy of a deuterated protein.
J Biomol NMR. 2010 Aug 29;
Authors: Tang M, Comellas G, Mueller LJ, Rienstra CM
High resolution (13)C-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 (15)N, (13)C', (13)Calpha and (13)Cbeta sites are resolved in (13)C-(13)C and (15)N-(13)C spectra, with significant...