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.

scholarly journals 15N-1H Residual Dipolar Coupling Analysis of Native and Alkaline-K79A Saccharomyces cerevisiae Cytochrome c

2003 ◽  
Vol 84 (6) ◽  
pp. 3917-3923 ◽  
Author(s):  
Michael Assfalg ◽  
Ivano Bertini ◽  
Paola Turano ◽  
A. Grant Mauk ◽  
Jay R. Winkler ◽  
...  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Cytochrome C ◽  
Dipolar Coupling ◽  
Residual Dipolar Coupling ◽  
Coupling Analysis

REDCAT: a residual dipolar coupling analysis tool

2004 ◽  
Vol 167 (2) ◽  
pp. 228-241 ◽  
Author(s):  
Homayoun Valafar ◽  
James H Prestegard
Keyword(s):  
Dipolar Coupling ◽  
Residual Dipolar Coupling ◽  
Analysis Tool ◽  
Coupling Analysis

scholarly journals Stretched Gelatin Phantom for Detection of Residual Dipolar Couplings in MR Spectra and Data Analysis of Carnosine

2016 ◽  
Vol 2016 ◽  
pp. 1-7
Author(s):  
Karel Bernášek ◽  
Marián Grocký ◽  
Martin Burian ◽  
Jan Lang
Keyword(s):  
Skeletal Muscle ◽  
Data Analysis ◽  
Residual Dipolar Couplings ◽  
Dipolar Coupling ◽  
Residual Dipolar Coupling ◽  
Dipolar Couplings ◽  
Peak Splitting ◽  
Gelatin Sample

Peak splitting due to the residual dipolar coupling (RDC) represents a potentially applicable spectral parameter for diagnostic purposes. Several of the skeletal muscle metabolites were previously reported to display the RDC splitting inin vivoMR spectra. We constructed anin vitromodel consisting of mechanically stretched gelatin cylinder soaked with the muscle metabolite carnosine. We describe the preparation procedure of an upscaled 50 mL stretched gelatin sample with carnosine that can be used as a phantom for setting-up and testing of spectroscopic measurements of RDC in a MR scanner. We also report on analysis of the RDC splittings in1H and13C high resolution MR spectra of carnosine.

scholarly journals Single scan TROSY and E.COSY suite of experiments for the measurement of residual dipolar couplings in proteins

2006 ◽  
Vol 20 (4) ◽  
pp. 153-167 ◽  
Author(s):  
Tommaso Eliseo ◽  
Mariana Gallo ◽  
Riccardo Melis ◽  
Maurizio Paci ◽  
Renzo Bazzo ◽  
...  
Keyword(s):  
Residual Dipolar Couplings ◽  
Dipolar Coupling ◽  
Residual Dipolar Coupling ◽  
Peak Position ◽  
Dipolar Couplings ◽  
Pulse Field ◽  
Modulation Method ◽  
Water Suppression ◽  
Field Gradients ◽  
The Difference

Simple modifications of the gradient enhanced version of the TROSY experiment allow to obtain four different spectra containing each one of the components of the H–N doublet in15N labelled proteins. By measuring the difference in peak position among these four spectra, residual dipolar coupling values can be obtained for medium sized proteins. This experiment, which exploits the use of pulse field gradients to select the15N coherence pathway, produces excellent results in terms of water suppression. Moreover, tuning of a single delay in the sequence reduces notably the presence of artifacts. The performance of this suite of experiments, that we called TEC (Trosy–E.Cosy) experiment, is tested against aJ-modulation method, inherently more accurate but more time consuming, for the accuracy in the observed values of residual dipolar couplings. For larger proteins, the use of this strategy allows to select the most favourable combination of peaks giving the sharpest signals.

Spatial structure of triglycine determined by the residual dipolar coupling analysis

2003 ◽  
Vol 25 (1) ◽  
pp. 113-119 ◽  
Author(s):  
V. V. Klochkov ◽  
B. I. Khairutdinov ◽  
A. V. Klochkov ◽  
V. G. Shtyrlin ◽  
R. A. Shaykhutdinov
Keyword(s):  
Spatial Structure ◽  
Dipolar Coupling ◽  
Residual Dipolar Coupling ◽  
Coupling Analysis

Determination of the spatial structure of glutathione by residual dipolar coupling analysis

2005 ◽  
Vol 43 (11) ◽  
pp. 948-951 ◽  
Author(s):  
Anton V. Klochkov ◽  
Bulat I. Khairutdinov ◽  
Murat S. Tagirov ◽  
Vladimir V. Klochkov
Keyword(s):  
Spatial Structure ◽  
Dipolar Coupling ◽  
Residual Dipolar Coupling ◽  
Coupling Analysis

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
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