Related ArticlesDetecting the "Afterglow" of (13)C NMR in Proteins Using Multiple Receivers.
J Am Chem Soc. 2010 Dec 2;
Authors: Kupc?e E, Kay LE, Freeman R
We show that the weak signal that remains after (13)C-detected experiments (the (13)C "afterglow") can still be measured with high sensitivity by proton detection. This is illustrated by the incorporation of two experiments, 2D (HA)CACO and 3D (HA)CA(CO)NNH, into a single pulse sequence that makes use of two receivers in parallel. In cases where the sensitivity is not limiting, such as applications to small proteins, the inclusion of the projection-reconstruction method permits the recording of both spectra in only 15 min. High-quality data sets for the 143 residue nuclease A inhibitor (2 °C, correlation time 17.5 ns) were obtained in 3 h, illustrating the utility of the method even in studies of moderately sized proteins.
PMID: 21126087 [PubMed - as supplied by publisher]
NMR with Multiple Receivers.
NMR with Multiple Receivers.
NMR with Multiple Receivers.
Top Curr Chem. 2011 Aug 12;
Authors: Kup?e E
Parallel acquisition NMR spectroscopy (PANSY) is used to detect simultaneously signals from up to four nuclear species, such as H-1, H-2, C-13, N-15, F-19 and P-31. The conventional COSY, TOCSY, HSQC, HMQC and HMBC pulse sequences have been adapted for such applications. Routine availability of NMR systems that incorporate multiple receivers has led to development of new types of NMR experiments. One such scheme named PANACEA allows unambiguous...
Detecting the “Afterglow” of 13C NMR in Proteins Using Multiple Receivers
Detecting the “Afterglow” of 13C NMR in Proteins Using Multiple Receivers
E?riks Kupc?e, Lewis E. Kay and Ray Freeman
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja1080025/aop/images/medium/ja-2010-080025_0002.gif
Journal of the American Chemical Society
DOI: 10.1021/ja1080025
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/YNH74d-9ntc
nmrlearner
Journal club
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12-03-2010 08:52 AM
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...
nmrlearner
Journal club
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10-22-2010 04:33 PM
[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
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...