Publication year: 2012 Source:Journal of Magnetic Resonance, Volume 215
Bingwu Yu, Hugo van Ingen, Subramanian Vivekanandan, Christoph Rademacher, Scott E. Norris, Darón I. Freedberg
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 interest. We report noticeable discrepancies between 1 J CH values measured with HSQC type pulse sequences in the 1H dimension from those measured in the 13C dimension for 17 sugars and show that these discrepancies arise from strong scalar coupling. In order to determine how to minimize errors in measuring 1 J CH, we analyze the strong coupling effects in detail using the product operator-formalism and spectral simulations based on the solution of the Liouville equation (not considering relaxation effects) in the presence of strong coupling. We report that the apparent 1 J CH measured with 2D HSQC-based sequences in either dimension can be in error by up to 4Hz and that the values measured in the 1H dimension can disagree with those in the 13C dimension by up to 7Hz. We demonstrate that spectral simulations can reproduce the errors induced by strong coupling and that these can be used to extract true 1 J CH values. We find that the 1 J CH values measured using a modified Z-filtered coupled HSQC are still affected by strong coupling. We conclude that spectral simulation yields accurate 1 J CH with errors as low as 1% in the presence of strong coupling. Graphical Abstract
Graphical abstract Highlights
? One-bond heteronuclear C–H couplings and RDCs may contain systematic errors. ? 1H–1H strong coupling causes these errors, which distort peak position. ? The errors are found in both 1H and 13C dimensions of a 2D HSQC. ? The errors are not due to digital resolution. ? Accurate coupling constants and RDCs should be obtained from fitting to simulated spectra where the effects of strong coupling are taken into account.
Identifying Guanosine Self Assembly at Natural Isotopic Abundance by High-Resolution 1H and 13C Solid-State NMR Spectroscopy
Identifying Guanosine Self Assembly at Natural Isotopic Abundance by High-Resolution 1H and 13C Solid-State NMR Spectroscopy
Amy L. Webber, Stefano Masiero, Silvia Pieraccini, Jonathan C. Burley, Andrew S. Tatton, Dinu Iuga, Tran N. Pham, Gian Piero Spada and Steven P. Brown
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja206516u/aop/images/medium/ja-2011-06516u_0007.gif
Journal of the American Chemical Society
DOI: 10.1021/ja206516u
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA...
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Fast NMR Data Acquisition From Bicelles Containing a Membrane-Associated Peptide at Natural-Abundance.
Fast NMR Data Acquisition From Bicelles Containing a Membrane-Associated Peptide at Natural-Abundance.
Fast NMR Data Acquisition From Bicelles Containing a Membrane-Associated Peptide at Natural-Abundance.
J Phys Chem B. 2011 Sep 22;
Authors: Yamamoto K, Vivekanandan S, Ramamoorthy A
Abstract
In spite of recent technological advances in NMR spectroscopy, its low sensitivity continues to be a major limitation particularly for the structural studies of membrane proteins. The need for a large quantity of a membrane protein and acquisition of...
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More AccurateJCHCoupling Measurement in the Presence ofJHHStrong Coupling in Natural Abundance
More AccurateJCHCoupling Measurement in the Presence ofJHHStrong Coupling in Natural Abundance
Publication year: 2011
Source: Journal of Magnetic Resonance, Available online 22 September 2011</br>
Bingwu*Yu, Hugo*van Ingen, Subramanian*Vivekanandan, Christoph*Rademacher, Scott E.*Norris, ...</br>
Jcouplings are essential for measuring RDCs (residual dipolar couplings), now routinely used to deduce molecular structure and dynamics of glycans and proteins. Accurate measurement ofJCHis critical for RDCs to reflect the true structure and dynamics in the molecule of interest. We report...
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[NMR paper] An NMR experiment for the accurate measurement of heteronuclear spin-lock relaxation
An NMR experiment for the accurate measurement of heteronuclear spin-lock relaxation rates.
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J Am Chem Soc. 2002 Sep 11;124(36):10743-53
Authors: Korzhnev DM, Skrynnikov NR, Millet O, Torchia DA, Kay LE
Rotating-frame relaxation rates, R(1)(rho), are often measured in NMR studies of protein dynamics. We show here that large systematic errors can be introduced into measured values of heteronuclear R(1)(rho) rates using schemes which are...
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[NMR paper] Extensive 1H NMR resonance assignment of proteins using natural abundance gradient-en
Extensive 1H NMR resonance assignment of proteins using natural abundance gradient-enhanced 13C-1H correlation spectroscopy.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Extensive 1H NMR resonance assignment of proteins using natural abundance gradient-enhanced 13C-1H correlation spectroscopy.
FEBS Lett. 1993 Nov 1;333(3):251-6
Authors: Medvedeva S, Simorre JP, Brutscher B, Guerlesquin F, Marion D
The reliability and completeness of 1H NMR resonance assignment can...
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[NMR paper] 1H- and natural abundance 15N-NMR studies of a derivative of a rabies glycoprotein fr
1H- and natural abundance 15N-NMR studies of a derivative of a rabies glycoprotein fragment.
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Biopolymers. 1991 May;31(6):713-23
Authors: Molinari H, Consonni R, Pegna M, Zetta L, Neri P, Niccolai N, Bonci A, Lozzi L, Rustici M, Scarselli M
Using a combination of one- and two-dimensional methods, 1H- and 15N-nmr spectroscopy has been employed to perform the complete assignment and the structural determination of the immunogenic...
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[NMR paper] Assignment of the natural abundance 13C spectrum of proteins using 13C 1H-detected he
Assignment of the natural abundance 13C spectrum of proteins using 13C 1H-detected heteronuclear multiple-bond correlation NMR spectroscopy: structural information and stereospecific assignments from two- and three-bond carbon-hydrogen coupling constants.
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Biochemistry. 1991 Oct 29;30(43):10457-66
...
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[NMR paper] Assignment of the natural abundance 13C spectrum of proteins using 13C 1H-detected he
Assignment of the natural abundance 13C spectrum of proteins using 13C 1H-detected heteronuclear multiple-bond correlation NMR spectroscopy: structural information and stereospecific assignments from two- and three-bond carbon-hydrogen coupling constants.
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Biochemistry. 1991 Oct 29;30(43):10457-66
...
More accurate 1JCH coupling measurement in the presence of 3JHH strong coupling in natural abundance
Graphical abstract Highlights 
Linear Mode
