Related ArticlesIn vivo 133Cs-NMR a probe for studying subcellular compartmentation and ion uptake in maize root tissue.
Biochim Biophys Acta. 1990 Sep 1;1054(2):169-75
Authors: Pfeffer PE, Rolin DB, Brauer D, Tu SI, Kumosinski TF
Three 133Cs-NMR signals were observed in the spectra of CsCl-perfused and CsCl-grown maize seedling root tips. Two relatively broad lower field resonances were assigned to the subcellular, compartmented Cs+ in the cytoplasm and vacuole, respectively. The rate of area increase of the broader cytoplasmic Cs resonance was about 9-times faster than that of the vacuolar signal during the first 300 min of tissue perfusion with CsCl. In addition, the spin lattice relaxation time of the cytoplasmic Cs resonance was approx. 3-times shorter than that of the extracellular resonance, while the Cs+ signal associated with the metabolically less active vacuolar compartment exhibited a relaxation time comparable to that of the extracellular signal. 133Cs spectra of excised, maize root tips and excised top sections of the root adjacent to the kernel, each grown in 10 mM CsCl showed a difference in the relative areas of the Cs resonance corresponding to the distinct cytoplasm/vacuole volume ratio of these well differentiated sections of the root. The high correlation of counterion concentration with 133Cs chemical shifts suggested that the larger downfield shift exhibited by the cytoplasmic confined Cs+ was due principally to the higher ionic strength and protein content in this compartment. Such observations indicate that 133Cs-NMR might be employed for studying ionic strength, and osmotic pressure associated chemical shifts and the transport properties of Cs+ (perhaps as an analogue for K+) in subcellular compartments of plant tissues.
[Question from NMRWiki Q&A forum] Tuning probe failed after a dual probe was replaced with a BBI probe
Tuning probe failed after a dual probe was replaced with a BBI probe
We generally use Dual to run 13C and BBI to run 2D. After changed the probe, the command "edhead" was used to set the probe. Put the sample tube, lock the solvent, and then type "atma" to tune the probe. We always do it like this, but now we can not tune the proton after installed the BBI probe (13C is OK). The dip can not be found by "atma", and "atmm" was also not work on forming a dip. What is the most possible reason for this error? How to solve it and avoid it in the future ? Thanks. (Instrument: Bruker 400 MHz,...
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08-23-2011 05:31 PM
[Stan NMR blog] Mercury in-vivo imaging?
Mercury in-vivo imaging?
Answer to a query about the feasibility of 199Hg MRI
Source: Stan blog library
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12-21-2010 02:14 AM
[NMR paper] Iron uptake by ferritin: NMR relaxometry studies at low iron loads.
Iron uptake by ferritin: NMR relaxometry studies at low iron loads.
Related Articles Iron uptake by ferritin: NMR relaxometry studies at low iron loads.
J Inorg Biochem. 1998 Sep;71(3-4):153-7
Authors: Vymazal J, Brooks RA, Bulte JW, Gordon D, Aisen P
Twenty ferritin samples were prepared at pH 6.5 with average loadings of 0-89 Fe atoms per molecule. Nuclear magnetic relaxation times T1 and T2 were measured at 3 degrees C, 23 degrees C, and at 37 degrees C and at field strength from 0.025 to 1.5 T. The field dependence, temperature dependence,...
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11-17-2010 11:15 PM
[NMR paper] Quantitation of metabolic compartmentation in hyperammonemic brain by natural abundan
Quantitation of metabolic compartmentation in hyperammonemic brain by natural abundance 13C-NMR detection of 13C-15N coupling patterns and isotopic shifts.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif Related Articles Quantitation of metabolic compartmentation in hyperammonemic brain by natural abundance 13C-NMR detection of 13C-15N coupling patterns and isotopic shifts.
Eur J Biochem. 1997 Feb 1;243(3):597-604
Authors: Lapidot A, Gopher A
In...
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08-22-2010 03:31 PM
[NMR paper] Quantitation of metabolic compartmentation in hyperammonemic brain by natural abundan
Quantitation of metabolic compartmentation in hyperammonemic brain by natural abundance 13C-NMR detection of 13C-15N coupling patterns and isotopic shifts.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif Related Articles Quantitation of metabolic compartmentation in hyperammonemic brain by natural abundance 13C-NMR detection of 13C-15N coupling patterns and isotopic shifts.
Eur J Biochem. 1997 Feb 1;243(3):597-604
Authors: Lapidot A, Gopher A
In...
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08-22-2010 03:03 PM
[NMR paper] Studying DNA-protein interactions using NMR.
Studying DNA-protein interactions using NMR.
Related Articles Studying DNA-protein interactions using NMR.
Trends Biotechnol. 1991 Mar;9(3):96-104
Authors: Russu IM
NMR spectroscopy is emerging as a powerful tool in molecular biology and biotechnology; one aspect of which is the use of one- and two-dimensional NMR methodologies to investigate the interactions of proteins with DNA. The dynamic and structural information which NMR can provide, on the changes in conformation and molecular flexibility, complements X-ray crystallography data and...
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08-21-2010 11:16 PM
In vivo protein NMR assignments by PR-NMR
Multidimensional NMR Spectroscopy for Protein Characterization and Assignment inside Cells
Patrick N. Reardon and Leonard D. Spicer*
Departments of Biochemistry and Radiology, Duke University Medical Center, Durham, North Carolina 27710
J. Am. Chem. Soc., 127 (31), 10848 -10849, 2005.
http://pubs.acs.org/isubscribe/journals/jacsat/127/i31/figures/ja053145kn00001.gif
Abstract:
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...
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08-03-2005 07:29 AM
2H NMR Spin Relaxation for studying RNA dynamics
A Suite of 2H NMR Spin Relaxation Experiments for the Measurement of RNA Dynamics
Pramodh Vallurupalli and Lewis E. Kay, J. Am. Chem. Soc.; 2005; 127 (18) pp 6893 - 6901
ABSTRACT:
A suite of (2)H-based spin relaxation NMR experiments is presented for the measurement of molecular dynamics in a site-specific manner in uniformly (13)C, randomly fractionally deuterated ( approximately 50%) RNA molecules. The experiments quantify (2)H R(1) and R(2) relaxation rates that can subsequently be analyzed to obtain information about dynamics on a pico- to nanosecond time scale. Sensitivity...