Residual Dipolar‐Coupling‐Based Conformational Comparison of Noncovalent Ubiquitin Homodimer with Covalently Linked Diubiquitin

ChemPhysChem ◽  
2020 ◽  
Vol 21 (9) ◽  
pp. 888-894
Author(s):  
A. Shine ◽  
J. Shenoy ◽  
Parvathy Jayan ◽  
A. C. Jiji ◽  
Vinesh Vijayan
Keyword(s):  
Dipolar Coupling ◽  
Residual Dipolar Coupling ◽  
Covalently Linked

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

Theoretical Analysis of Residual Dipolar Coupling Patterns in Regular Secondary Structures of Proteins

2003 ◽  
Vol 125 (41) ◽  
pp. 12520-12526 ◽  
Author(s):  
Alessandro Mascioni ◽  
Gianluigi Veglia
Keyword(s):  
Theoretical Analysis ◽  
Dipolar Coupling ◽  
Residual Dipolar Coupling ◽  
Secondary Structures

Configurational Analysis by Residual Dipolar Coupling Driven Floating Chirality Distance Geometry Calculations

2018 ◽  
Vol 24 (52) ◽  
pp. 13918-13930 ◽  
Author(s):  
Stefan Immel ◽  
Matthias Köck ◽  
Michael Reggelin
Keyword(s):  
Dipolar Coupling ◽  
Distance Geometry ◽  
Residual Dipolar Coupling ◽  
Configurational Analysis

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.

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

A novel strategy to determine protein structures using exclusively residual dipolar coupling

2008 ◽  
Vol 29 (10) ◽  
pp. 1640-1649 ◽  
Author(s):  
Thenmalarchelvi Rathinavelan ◽  
Wonpil Im
Keyword(s):  
Dipolar Coupling ◽  
Protein Structures ◽  
Residual Dipolar Coupling ◽  
Novel Strategy

PROTEIN FOLD RECOGNITION THROUGH APPLICATION OF RESIDUAL DIPOLAR COUPLING DATA

2003 ◽  
Author(s):  
Y. QU ◽  
J.-T. GUO ◽  
V. OLMAN ◽  
Y. XU
Keyword(s):  
Dipolar Coupling ◽  
Residual Dipolar Coupling ◽  
Fold Recognition ◽  
Protein Fold ◽  
Protein Fold Recognition
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