Related Articles23Na NMR spectroscopy of free Na+ in the halotolerant bacterium Brevibacterium sp. and Escherichia coli.
Microbiology. 1995 Mar;141 ( Pt 3):729-36
Authors: Nagata S, Adachi K, Shirai K, Sano H
23Na NMR spectroscopy was used to determine free Na+ concentrations in a halotolerant bacterium, Brevibacterium sp., and Escherichia coli. The internal Na+ concentration of both strains depended little on the growth phases and was unchanged after 5 d storage at 2 degrees C. In Brevibacterium sp. the level of intracellular sodium increased gradually at higher extracellular NaCl concentrations in both the presence and absence of yeast extract in the growth medium. E. coli cells accumulated a higher concentration of free Na+ than those of Brevibacterium sp. The change of Na+ concentration in both strains was inverse to that of growth rate. When appropriate amounts of osmoprotectants (proline, glycine betaine, or gamma-aminobutyrate) were added with the NaCl, internal free Na+ levels in Brevibacterium sp. were lowered, but those of E. coli were unchanged. While addition of KCl to medium containing NaCl increased the intracellular level of free Na+, the total sodium concentration in the cells remained unchanged, indicating that sodium that had been bound or attached was made free in the cytosol. In Brevibacterium sp. grown in the presence of 0.5 M NaCl, free and bound sodium concentrations in the cytosol were estimated to be 0.14 and 0.23 mumol (mg protein)-1, respectively. As a result, visibility by 23Na NMR was 38%.
[NMR software blog] Free for 1 Year
Free for 1 Year
I said to myself: "What if I return to the original concept of the blog, that is to write reviews of existing NMR software"?
I remembered there was one I had never tried. It's called NPNMR (where NP stays for: "Natural Products") and the web site has been in existence for a number of years, though I only heard about it from Google. The NMR wiki ignores it. I remembered there was a freeware version; I wanted to try it. The installation was successful. License was more problematic. The free license is not forever. It only lasts one year, starting from January 1, 2010. In...
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01-18-2011 02:44 AM
A new method for the determination of free L: -carnitine in serum samples based on high field single quantum coherence filtering (1)H-NMR spectroscopy.
A new method for the determination of free L: -carnitine in serum samples based on high field single quantum coherence filtering (1)H-NMR spectroscopy.
A new method for the determination of free L: -carnitine in serum samples based on high field single quantum coherence filtering (1)H-NMR spectroscopy.
Anal Bioanal Chem. 2011 Jan 11;
Authors: Tsiafoulis CG, Exarchou V, Tziova PP, Bairaktari E, Gerothanassis IP, Troganis AN
The rapid and accurate determination of specific metabolites present in biofluids is a very demanding task which is essential...
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01-12-2011 11:11 AM
[NMR paper] High pressure nmr study of dihydrofolate reductase from a deep-sea bacterium Moritell
High pressure nmr study of dihydrofolate reductase from a deep-sea bacterium Moritella profunda.
Related Articles High pressure nmr study of dihydrofolate reductase from a deep-sea bacterium Moritella profunda.
Cell Mol Biol (Noisy-le-grand). 2004 Jun;50(4):311-6
Authors: Hata K, Kono R, Fujisawa M, Kitahara R, Kamatari YO, Akasaka K, Xu Y
We have investigated the effect of pressure and temperature on the structural and thermodynamic stability of a protein dihydrofolate reductase from a deep-sea bacterium Moritella profunda in its folate-bound...
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11-24-2010 09:51 PM
[NMR paper] Solution NMR structure of the cold-shock protein from the hyperthermophilic bacterium
Solution NMR structure of the cold-shock protein from the hyperthermophilic bacterium Thermotoga maritima.
Related Articles Solution NMR structure of the cold-shock protein from the hyperthermophilic bacterium Thermotoga maritima.
Eur J Biochem. 2001 May;268(9):2527-39
Authors: Kremer W, Schuler B, Harrieder S, Geyer M, Gronwald W, Welker C, Jaenicke R, Kalbitzer HR
Cold-shock proteins (Csps) are a subgroup of the cold-induced proteins preferentially expressed in bacteria and other organisms on reduction of the growth temperature below the...
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11-19-2010 08:32 PM
[NMR paper] Solution structure of the oxidized Fe7S8 ferredoxin from the thermophilic bacterium B
Solution structure of the oxidized Fe7S8 ferredoxin from the thermophilic bacterium Bacillus schlegelii by 1H NMR spectroscopy.
Related Articles Solution structure of the oxidized Fe7S8 ferredoxin from the thermophilic bacterium Bacillus schlegelii by 1H NMR spectroscopy.
Biochemistry. 1998 Jul 7;37(27):9812-26
Authors: Aono S, Bentrop D, Bertini I, Donaire A, Luchinat C, Niikura Y, Rosato A
The solution structure of the paramagnetic seven-iron ferredoxin from Bacillus schlegelii in its oxidized form has been determined by 1H NMR. The protein,...
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11-17-2010 11:15 PM
[NMR paper] Hydration water molecules of nucleotide-free RNase T1 studied by NMR spectroscopy in
Hydration water molecules of nucleotide-free RNase T1 studied by NMR spectroscopy in solution.
Related Articles Hydration water molecules of nucleotide-free RNase T1 studied by NMR spectroscopy in solution.
J Biomol NMR. 1998 Jan;11(1):1-15
Authors: Pfeiffer S, Spitzner N, Löhr F, Rüterjans H
The hydration of uncomplexed RNase T1 was investigated by NMR spectroscopy at pH 5.5 and 313 K. Two-dimensional heteronuclear NOE and ROE difference experiments were employed to determine the spatial proximity and the residence times of water molecules at...
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11-17-2010 11:06 PM
Study of effect of molecular mobility in chromatophore membranes of the bacterium E.
Study of effect of molecular mobility in chromatophore membranes of the bacterium E. shaposhnikovii on processes of photoinduced electron transport using the NMR-spin-echo method with isotope substitution and dehydration.
Related Articles Study of effect of molecular mobility in chromatophore membranes of the bacterium E. shaposhnikovii on processes of photoinduced electron transport using the NMR-spin-echo method with isotope substitution and dehydration.
Biochemistry (Mosc). 2010 Apr;75(4):423-7
Authors: Chamorovsky CS, Chamorovsky SK, Knox PP
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