A very interesting note* has recently been published in Concepts in Magnetic Resonance Part A by Joseph Hornak (generous provider of the two excellent free online text books, The Basics of NMR and The Basics of MRI ). In this work, it is demonstrated that an MRI scanner can be used to reproduce an image of printed text. The technique is based on the fact that the toner used to print text contains ferromagnetic particles and when placed in the uniform magnetic field of an MRI magnet, the magnetic field near the ferromagnetic toner is distorted. The "sample" is prepared by placing the printed page face up on a polycarbonate plate and covering it with a very thin sheet of polyethylene. The polyethylene is covered with water (doped with CuSO4 as a relaxation agent). The "sample" is placed in the magnet such that the plane of the page is perpendicular to the magnetic field. The text is "scanned" by taking a 2D proton MR image of a slice of the water near the surface of the polyethylene. The distortion in the magnetic field due to the ferromagnetic toner renders the text visible in the 2D magnetic resonance image. This is demonstrated in the figure below (from the reference) where a 2.5 mm thick slice above the polyethylene was imaged. The text was printed in #36 Arial font. The author speculates that this technique may be applied to the analysis of paintings.
* Joseph P. Hornak, "Magnetic Resonance Imaging of Printed Text", Concepts in Magnetic Resonance Part A.36A, 347 (2010).
Mechanically, Magnetically, and "Rotationally Aligned" Membrane Proteins in Phospholi
Mechanically, Magnetically, and "Rotationally Aligned" Membrane Proteins in Phospholipid Bilayers Give Equivalent Angular Constraints for NMR Structure Determination.
Related Articles Mechanically, Magnetically, and "Rotationally Aligned" Membrane Proteins in Phospholipid Bilayers Give Equivalent Angular Constraints for NMR Structure Determination.
J Phys Chem B. 2010 Oct 20;
Authors: Park SH, Das BB, De Angelis AA, Scrima M, Opella SJ
The native environment for membrane proteins is the highly asymmetric phospholipid bilayer, and this has a large...
[Question from NMRWiki Q&A forum] What is the easiest way to emulate the "array" command from VNMR in XWINNMR/TOPSPIN?
What is the easiest way to emulate the "array" command from VNMR in XWINNMR/TOPSPIN?
What is the easiest way to emulate the "array" command from VNMR in XWINNMR/TOPSPIN? I recently moved from a lab using a Varian (Unity plus 500) with VNMR 6.whatever to a lab with only Bruker (AVANCE 300/400/500) spectrometers available. I am used to using the "array" caommand in VNMR and viewing the spectra with "dssa" or "dssh." I don't know a convenient way to do the same thing in XWINNMR. I know there are some AU programs but I'm not sure what they all do or if what I want is available. I tried...
nmrlearner
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09-24-2010 07:36 PM
[NMR paper] NMR structure of a stable "OB-fold" sub-domain isolated from staphylococcal nuclease.
NMR structure of a stable "OB-fold" sub-domain isolated from staphylococcal nuclease.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles NMR structure of a stable "OB-fold" sub-domain isolated from staphylococcal nuclease.
J Mol Biol. 1995 Jul 7;250(2):134-43
Authors: Alexandrescu AT, Gittis AG, Abeygunawardana C, Shortle D
Similar folds often occur in proteins with dissimilar sequences. The OB-fold forms a part of the structures of at least seven non-homologous proteins...
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08-22-2010 03:50 AM
Postdoctoral Position "Solution Dynamics of Protein Kinases" in New York
Postdoctoral Position "Solution Dynamics of Protein Kinases" in New York
A postdoctoral position to study the solution dynamics and structure
of protein kinases is available on a NIH funded project (REF#:
HS-R-6453-10-08-S). Our group is interested in how static and dynamic
changes of protein structure affect the activity of protein kinases.
We combine X-ray crystallography, NMR and ligand binding kinetics with
collaborative molecular dynamic studies (See e.g. ref 1 and 2). Our
research group is located at Stony Brook University in a highly
interactive environment with the New York...