... way to measure this coupling constant in unlabeled proteins is fitting
20/03/2014 12:45:23 PM GMT
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On the calculation of 3Jαβ-coupling constants for side chains in proteins
On the calculation of 3Jαβ-coupling constants for side chains in proteins
Abstract Structural knowledge about proteins is mainly derived from values of observables, measurable in NMR spectroscopic or X-ray diffraction experiments, i.e. absorbed or scattered intensities, through theoretically derived relationships between structural quantities such as atom positions or torsional angles on the one hand and observable quantities such as squared structure factor amplitudes, NOE intensities or 3 J-coupling constants on the other. The standardly used relation connecting 3 J-couplings...
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06-25-2012 04:41 AM
More accurate 1JCH coupling measurement in the presence of 3JHH strong coupling in natural abundance
More accurate 1JCH coupling measurement in the presence of 3JHH strong coupling in natural abundance
Publication year: 2012
Source:Journal of Magnetic Resonance, Volume 215</br>
Bingwu Yu, Hugo van Ingen, Subramanian Vivekanandan, Christoph Rademacher, Scott E. Norris, Darón I. Freedberg</br>
J couplings are essential for measuring RDCs (residual dipolar couplings), now routinely used to deduce molecular structure and dynamics of glycans and proteins. Accurate measurement of 1 J CH is critical for RDCs to reflect the true structure and dynamics in the molecule of...
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03-09-2012 09:16 AM
The Use of Residual Dipolar Coupling in Studying Proteins by NMR.
The Use of Residual Dipolar Coupling in Studying Proteins by NMR.
The Use of Residual Dipolar Coupling in Studying Proteins by NMR.
Top Curr Chem. 2011 Sep 28;
Authors: Chen K, Tjandra N
Abstract
The development of residual dipolar coupling (RDC) in protein NMR spectroscopy, over a decade ago, has become a useful and almost routine tool for accurate protein solution structure determination. RDCs provide orientation information of magnetic dipole-dipole interaction vectors within a common reference frame. Its measurement requires a...
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09-30-2011 06:00 AM
The Use of Residual Dipolar Coupling in Studying Proteins by NMR.
The Use of Residual Dipolar Coupling in Studying Proteins by NMR.
The Use of Residual Dipolar Coupling in Studying Proteins by NMR.
Top Curr Chem. 2011 Sep 28;
Authors: Chen K, Tjandra N
Abstract
The development of residual dipolar coupling (RDC) in protein NMR spectroscopy, over a decade ago, has become a useful and almost routine tool for accurate protein solution structure determination. RDCs provide orientation information of magnetic dipole-dipole interaction vectors within a common reference frame. Its measurement requires a...
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09-30-2011 05:59 AM
[Question from NMRWiki Q&A forum] How can I calculate a carbon-proton coupling constant for a molecule?
How can I calculate a carbon-proton coupling constant for a molecule?
I'm trying to explain a missing HMBC peak, and having a coupling constant less than 10 Hz would do that nicely. It's a formamidine derivative with a 3 bond correlation N=CHNC The C is a quaternary carbon in a benzene ring. Any help would be appreciated.
Check if somebody has answered this question on NMRWiki QA forum
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02-04-2011 07:12 PM
[NMR paper] Intein-based biosynthetic incorporation of unlabeled protein tags into isotopically l
Intein-based biosynthetic incorporation of unlabeled protein tags into isotopically labeled proteins for NMR studies.
Related Articles Intein-based biosynthetic incorporation of unlabeled protein tags into isotopically labeled proteins for NMR studies.
Nat Biotechnol. 2005 Jun;23(6):736-40
Authors: Züger S, Iwai H
Segmental isotopic labeling of proteins using protein ligation is a recently established in vitro method for incorporating isotopes into one domain or region of a protein to reduce the complexity of NMR spectra, thereby facilitating...
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11-25-2010 08:21 PM
[NMR paper] An efficient NMR experiment for analyzing sugar-puckering in unlabeled DNA: applicati
An efficient NMR experiment for analyzing sugar-puckering in unlabeled DNA: application to the 26-kDa dead ringer-DNA complex.
Related Articles An efficient NMR experiment for analyzing sugar-puckering in unlabeled DNA: application to the 26-kDa dead ringer-DNA complex.
J Magn Reson. 2001 Dec;153(2):262-6
Authors: Iwahara J, Wojciak JM, Clubb RT
We present a new NMR experiment for estimating the type and degree of sugar-puckering in high-molecular-weight unlabeled DNA molecules. The experiment consists of a NOESY sequence preceded by a...
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11-19-2010 08:44 PM
[NMR paper] A structural mode-coupling approach to 15N NMR relaxation in proteins.
A structural mode-coupling approach to 15N NMR relaxation in proteins.
Related Articles A structural mode-coupling approach to 15N NMR relaxation in proteins.
J Am Chem Soc. 2001 Apr 4;123(13):3055-63
Authors: Tugarinov V, Liang Z, Shapiro YE, Freed JH, Meirovitch E
The two-body Slowly Relaxing Local Structure (SRLS) model was applied to (15)N NMR spin relaxation in proteins and compared with the commonly used original and extended model-free (MF) approaches. In MF, the dynamic modes are assumed to be decoupled, local ordering at the N-H sites...