Ultra-high resolution in MAS solid-state NMR of perdeuterated proteins: Implications for Structure and Dynamics
Ultra-high resolution in MAS solid-state NMR of perdeuterated proteins: Implications for Structure and Dynamics
Publication year: 2012
Source: Journal of Magnetic Resonance, Available online 5 January 2012</br>
Bernd*Reif</br>
http://www.sciencedirect.com/cache/MiamiImageURL/1-s2.0-S1090780711005969-fx1.sml</br></br></br>
Source: Journal of Magnetic Resonance
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01-07-2012 03:12 PM
Ultra High-Resolution NMR: Sustained Induction Decays of Long-Lived Coherences
Ultra High-Resolution NMR: Sustained Induction Decays of Long-Lived Coherences
Aure?lien Bornet, Sami Jannin, J. A. (Ton) Konter, Patrick Hautle, Ben van den Brandt and Geoffrey Bodenhausen
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja2052792/aop/images/medium/ja-2011-052792_0005.gif
Journal of the American Chemical Society
DOI: 10.1021/ja2052792
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/F3VMiSJp4h4
High resolution NMR spectroscopy of nanocrystalline proteins at ultra-high magnetic field
High resolution NMR spectroscopy of nanocrystalline proteins at ultra-high magnetic field
Abstract Magic-angle spinning (MAS) solid-state NMR (SSNMR) spectroscopy of uniformly-13C,15N labeled protein samples provides insight into atomic-resolution chemistry and structure. Data collection efficiency has advanced remarkably in the last decade; however, the study of larger proteins is still challenged by relatively low resolution in comparison to solution NMR. In this study, we present a systematic analysis of SSNMR protein spectra acquired at 11.7, 17.6 and 21.1 Tesla (1H frequencies of...
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01-09-2011 12:46 PM
[NMR paper] Ultra-high-field MAS NMR assay of a multispin labeled ligand bound to its G-protein r
Ultra-high-field MAS NMR assay of a multispin labeled ligand bound to its G-protein receptor target in the natural membrane environment: electronic structure of the retinylidene chromophore in rhodopsin.
Related Articles Ultra-high-field MAS NMR assay of a multispin labeled ligand bound to its G-protein receptor target in the natural membrane environment: electronic structure of the retinylidene chromophore in rhodopsin.
Biochemistry. 2001 Mar 20;40(11):3282-8
Authors: Verhoeven MA, Creemers AF, Bovee-Geurts PH, De Grip WJ, Lugtenburg J, de Groot HJ
...
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11-19-2010 08:32 PM
[NMRwiki tweet] nmrwiki: Why HCCH TOCSY does not work for whole aromatic side chains? #nmrhttp://qa.n
nmrwiki: Why HCCH TOCSY does not work for whole aromatic side chains? #nmrhttp://qa.nmrwiki.org/question/199/
nmrwiki: Why HCCH TOCSY does not work for whole aromatic side chains? #nmrhttp://qa.nmrwiki.org/question/199/
Source: NMRWiki tweets