NMR spectroscopy could be used to save the lives of children with septic shock by revealing the tell-tale profile of metabolites associated with the severest cases of this condition.
[Question from NMRWiki Q&A forum] Automatically Saving VNMR6.1 Data Post-Acquisition
Automatically Saving VNMR6.1 Data Post-Acquisition
Does anyone know of a convenient way to automatically save data in VNMR6.1? Occasionally, if an experiment is left to run overnight, I am not able to reach the terminal in time before another user runs an experiment. I would like to be able to tell the software to save the data once acquisition is complete.
Thank you for your time!
Check if somebody has answered this question on NMRWiki QA forum
nmrlearner
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05-05-2012 12:14 AM
[NMR Geek blog] Saving Projects in Sparky
Saving Projects in Sparky
I found a bug in Sparky (NMR analysis software) – am not sure if its a known bug or not! If you have multiple spectra open and you save entire work as a project, and then if you close and re-open the project, Sparky will not let you visualize those spectra which were minimized before
Full story can be found on the NMR geek blog
[NMR paper] Solution NMR structure of ribosome-binding factor A (RbfA), a cold-shock adaptation p
Solution NMR structure of ribosome-binding factor A (RbfA), a cold-shock adaptation protein from Escherichia coli.
Related Articles Solution NMR structure of ribosome-binding factor A (RbfA), a cold-shock adaptation protein from Escherichia coli.
J Mol Biol. 2003 Mar 21;327(2):521-36
Authors: Huang YJ, Swapna GV, Rajan PK, Ke H, Xia B, Shukla K, Inouye M, Montelione GT
Ribosome-binding factor A (RbfA) from Escherichia coli is a cold-shock adaptation protein. It is essential for efficient processing of 16S rRNA and is suspected to interact with...
nmrlearner
Journal club
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11-24-2010 09:01 PM
[NMR paper] NMR of hydrogen bonding in cold-shock protein A and an analysis of the influence of c
NMR of hydrogen bonding in cold-shock protein A and an analysis of the influence of crystallographic resolution on comparisons of hydrogen bond lengths.
Related Articles NMR of hydrogen bonding in cold-shock protein A and an analysis of the influence of crystallographic resolution on comparisons of hydrogen bond lengths.
Protein Sci. 2001 Sep;10(9):1856-68
Authors: Alexandrescu AT, Snyder DR, Abildgaard F
Hydrogen bonding in cold-shock protein A of Escherichia coli has been investigated using long-range HNCO spectroscopy. Nearly half of the...
nmrlearner
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11-19-2010 08:44 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...
nmrlearner
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11-19-2010 08:32 PM
[NMR paper] Solution NMR structure and backbone dynamics of the major cold-shock protein (CspA) f
Solution NMR structure and backbone dynamics of the major cold-shock protein (CspA) from Escherichia coli: evidence for conformational dynamics in the single-stranded RNA-binding site.
Related Articles Solution NMR structure and backbone dynamics of the major cold-shock protein (CspA) from Escherichia coli: evidence for conformational dynamics in the single-stranded RNA-binding site.
Biochemistry. 1998 Aug 4;37(31):10881-96
Authors: Feng W, Tejero R, Zimmerman DE, Inouye M, Montelione GT
The major cold-shock protein (CspA) from Escherichia...
nmrlearner
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11-17-2010 11:15 PM
[NMR paper] NMR assignments for acid-denatured cold shock protein A.
NMR assignments for acid-denatured cold shock protein A.
Related Articles NMR assignments for acid-denatured cold shock protein A.
J Biomol NMR. 1998 May;11(4):461-2
Authors: Alexandrescu AT, Rathgeb-Szabo K