13C CPMAS NMR spectra of solid proton-exchanging p-substituted benzoylacetones: observation of13C,35,37Cl residual dipolar coupling in the p-chloro derivative

1993 ◽  
pp. 1253-1254 ◽  
Author(s):  
Raquel M. Cravero ◽  
Manuel González-Sierra ◽  
Claudio Fernández ◽  
Alejandro C. Olivieri
Keyword(s):  
Nmr Spectra ◽  
Dipolar Coupling ◽  
Residual Dipolar Coupling ◽  
13C Cpmas Nmr ◽  
Chloro Derivative

Variable-Field Study of 13C,35,37Cl Residual Dipolar Coupling in the 13C CPMAS NMR Spectra of Pyrazole Derivatives

1994 ◽  
Vol 98 (20) ◽  
pp. 5207-5211 ◽  
Author(s):  
Alejandro C. Olivieri ◽  
Jose Elguero ◽  
Isabel Sobrados ◽  
Pilar Cabildo ◽  
Rosa M. Claramunt
Keyword(s):  
Field Study ◽  
Nmr Spectra ◽  
Dipolar Coupling ◽  
Residual Dipolar Coupling ◽  
Pyrazole Derivatives ◽  
13C Cpmas Nmr ◽  
Variable Field

Analysis of13C,14N residual dipolar coupling in the13C CP/MAS NMR spectra of ribonucleosides

1988 ◽  
Vol 26 (4) ◽  
pp. 281-286 ◽  
Author(s):  
Alejandro C. Olivieri ◽  
Lucio Frydman ◽  
Mariano Grasselli ◽  
Luis E. Diaz
Keyword(s):  
Nmr Spectra ◽  
Dipolar Coupling ◽  
Residual Dipolar Coupling ◽  
Mas Nmr ◽  
Cp Mas Nmr

scholarly journals Structure-Free Validation of Residual Dipolar Coupling and Paramagnetic Relaxation Enhancement Measurements of Disordered Proteins

Biochemistry ◽  
2015 ◽  
Vol 54 (46) ◽  
pp. 6876-6886 ◽  
Author(s):  
Francisco N. Newby ◽  
Alfonso De Simone ◽  
Maho Yagi-Utsumi ◽  
Xavier Salvatella ◽  
Christopher M. Dobson ◽  
...  
Keyword(s):  
Dipolar Coupling ◽  
Residual Dipolar Coupling ◽  
Paramagnetic Relaxation ◽  
Paramagnetic Relaxation Enhancement ◽  
Disordered Proteins

scholarly journals Analysis of Artifacts Caused by Pulse Imperfections in CPMG Pulse Trains in NMR Relaxation Dispersion Experiments

2018 ◽  
Vol 4 (3) ◽  
pp. 33 ◽  
Author(s):  
Tsuyoshi Konuma ◽  
Aritaka Nagadoi ◽  
Jun-ichi Kurita ◽  
Takahisa Ikegami
Keyword(s):  
Dipolar Coupling ◽  
Residual Dipolar Coupling ◽  
Nmr Relaxation ◽  
Relaxation Dispersion ◽  
Conformational Exchange ◽  
Resonance Effects ◽  
Pulse Trains ◽  
At Resonance ◽  
Selective Inversion ◽  
Resonance Relaxation

Nuclear magnetic resonance relaxation dispersion (rd) experiments provide kinetics and thermodynamics information of molecules undergoing conformational exchange. Rd experiments often use a Carr-Purcell-Meiboom-Gill (CPMG) pulse train equally separated by a spin-state selective inversion element (U-element). Even with measurement parameters carefully set, however, parts of 1H–15N correlations sometimes exhibit large artifacts that may hamper the subsequent analyses. We analyzed such artifacts with a combination of NMR measurements and simulation. We found that particularly the lowest CPMG frequency (νcpmg) can also introduce large artifacts into amide 1H–15N and aromatic 1H–13C correlations whose 15N/13C resonances are very close to the carrier frequencies. The simulation showed that the off-resonance effects and miscalibration of the CPMG π pulses generate artifact maxima at resonance offsets of even and odd multiples of νcpmg, respectively. We demonstrate that a method once introduced into the rd experiments for molecules having residual dipolar coupling significantly reduces artifacts. In the method the 15N/13C π pulse phase in the U-element is chosen between x and y. We show that the correctly adjusted sequence is tolerant to miscalibration of the CPMG π pulse power as large as ±10% for most amide 15N and aromatic 13C resonances of proteins.

scholarly journals The Flexibility of Oligosaccharides Unveiled Through Residual Dipolar Coupling Analysis

2021 ◽  
Vol 8 ◽  
Author(s):  
Ana Poveda ◽  
Giulio Fittolani ◽  
Peter H. Seeberger ◽  
Martina Delbianco ◽  
Jesús Jiménez-Barbero
Keyword(s):  
Residual Dipolar Couplings ◽  
Biological Function ◽  
Dipolar Coupling ◽  
Residual Dipolar Coupling ◽  
Relative Orientation ◽  
Coupling Analysis ◽  
Conformational Dynamic ◽  
Glycan Chain ◽  
Chemical Shift Degeneracy ◽  
Oligosaccharide Structures

The intrinsic flexibility of glycans complicates the study of their structures and dynamics, which are often important for their biological function. NMR has provided insights into the conformational, dynamic and recognition features of glycans, but suffers from severe chemical shift degeneracy. We employed labelled glycans to explore the conformational behaviour of a β(1-6)-Glc hexasaccharide model through residual dipolar couplings (RDCs). RDC delivered information on the relative orientation of specific residues along the glycan chain and provided experimental clues for the existence of certain geometries. The use of two different aligning media demonstrated the adaptability of flexible oligosaccharide structures to different environments.

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