COSY Cross-Peaks from1H−1H Dipolar Couplings in NMR Spectra of Field Oriented Oligosaccharides

1998 ◽  
Vol 120 (36) ◽  
pp. 9366-9367 ◽  
Author(s):  
P. J. Bolon ◽  
J. H. Prestegard
Keyword(s):  
Nmr Spectra ◽  
Dipolar Couplings

Deuterium Quadrupolar Parameters from 1H and 2H NMR Spectra for Pyridine-d5, Benzonitrile-d5 and Chlorobenzene-d5 Using Liquid Crystal Solvents

1986 ◽  
Vol 41 (1-2) ◽  
pp. 431-435 ◽  
Author(s):  
R. Ambrosetti ◽  
D. Catalano ◽  
C. Forte ◽  
C. A. Veracini
Keyword(s):  
Liquid Crystal ◽  
Nmr Spectra ◽  
Order Parameters ◽  
Dipolar Couplings ◽  
Coupling Constants ◽  
2H Nmr ◽  
H Nmr ◽  
Quadrupolar Coupling ◽  
Asymmetry Parameters ◽  
Quadrupolar Splittings

T he quadrupolar coupling constants (DQCC) and the asymmetry parameters (η) for the ortho, meta and para deuterons in pyridine-d5, benzonitrile-d5 and chlorobenzene-d5 were determined by NMR spectroscopy in oriented phases. The 1H and 2H NMR spectra were recorded in the following solutions in liquid crystal solvents: pyridine + pyridine-d5 in PCH , in ZLI 1167 and in EBBA; benzonitrile + benzonitrile-d5 and chlorobenzene + chlorobenzene-d5 in the same solvents.The order parameters of the non-deuterated solutes in the various solutions were calculated using the dipolar couplings of the proton spectra and the rα structures taken from the literature. The same order parameters were assumed to describe also the orientation of the deuterated solute in the corresponding solutions.Each 2H spectrum yielded three quadrupolar splittings for the three different deuterated positions in the labelled solute. The splittings from the three different solutions of the same solute, together with the order parameters and the rα structure, were used to determine DQCC and η of the ortho, meta and para deuterons (Pyridine-d5: DQCCortho= 183(1) kHz, ηortho = 0.030(5), DQCCmeta = 185(1) kHz, ηmeta = 0.030(10), DQCCpara = 188(6) kHz, ηpara = 0.01(5). Benzonitrile-d5: DQCCortho = 171(12) kHz, ηortho = 0.07(3), DQCCmeta = 175(12) kHz, ηmeta = 0.05(3), DQCCpara = 176(4) kHz, ηpara = 0.10(7). Chlorobenzene-d5: DQCCortho = 180(2) kHz, ηortho = 0.06(1), DQCCmeta = 174(2) kHz, ηmeta = 0.09(3), DQCCpara= 182(4) kHz, ηPara = 0.06(4)). The results are discussed, as well as the limits and possibilities of the method used.

Measurement ofJand Dipolar Couplings from Simplified Two-Dimensional NMR Spectra

1998 ◽  
Vol 131 (2) ◽  
pp. 373-378 ◽  
Author(s):  
Marcel Ottiger ◽  
Frank Delaglio ◽  
Ad Bax
Keyword(s):  
Nmr Spectra ◽  
Dipolar Couplings ◽  
Two Dimensional

Paramagpy: Software for Fitting Magnetic Susceptibility Tensors Using Paramagnetic Effects Measured in NMR Spectra

2019 ◽  
Author(s):  
Henry Orton ◽  
Thomas Huber ◽  
Gottfried Otting
Keyword(s):  
Experimental Data ◽  
Magnetic Susceptibility ◽  
Nmr Spectra ◽  
Residual Dipolar Couplings ◽  
Paramagnetic Relaxation ◽  
Dipolar Couplings ◽  
Paramagnetic Susceptibility ◽  
Pseudocontact Shifts ◽  
Seamless Transition ◽  
Paramagnetic Relaxation Enhancements

Paramagpy is a python module for calculating paramagnetic effects in NMR spectra of proteins. This currently includes fitting of paramagnetic susceptibility tensors to experimental data associated with pseudocontact shifts (PCS) residual dipolar couplings (RDC), paramagnetic relaxation enhancements (PRE) and cross-correlated relaxation (CCR). A GUI allows easy viewing of data and seamless transition between PCS/RDC/PRE/CCR calculations.<br><br>

scholarly journals Structure determination of membrane proteins by NMR spectroscopy

2002 ◽  
Vol 80 (5) ◽  
pp. 597-604 ◽  
Author(s):  
S J Opella ◽  
A Nevzorov ◽  
M F Mesleh ◽  
F M Marassi
Keyword(s):  
Nmr Spectroscopy ◽  
Chemical Shift ◽  
Membrane Proteins ◽  
Structure Determination ◽  
Nuclear Spin ◽  
Nmr Spectra ◽  
Dipolar Couplings ◽  
Solution Nmr ◽  
Two Dimensional ◽  
Spin Interactions

Current strategies for determining the structures of membrane proteins in lipid environments by NMR spectroscopy rely on the anisotropy of nuclear spin interactions, which are experimentally accessible through experiments performed on weakly and completely aligned samples. Importantly, the anisotropy of nuclear spin interactions results in a mapping of structure to the resonance frequencies and splittings observed in NMR spectra. Distinctive wheel-like patterns are observed in two-dimensional 1H–15N heteronuclear dipolar/15N chemical shift PISEMA (polarization inversion spin-exchange at the magic angle) spectra of helical membrane proteins in highly aligned lipid bilayer samples. One-dimensional dipolar waves are an extension of two-dimensional PISA (polarity index slant angle) wheels that map protein structures in NMR spectra of both weakly and completely aligned samples. Dipolar waves describe the periodic wave-like variations of the magnitudes of the heteronuclear dipolar couplings as a function of residue number in the absence of chemical shift effects. Since weakly aligned samples of proteins display these same effects, primarily as residual dipolar couplings, in solution NMR spectra, this represents a convergence of solid-state and solution NMR approaches to structure determination.Key words: NMR spectroscopy, protein structure, dipolar couplings, membrane proteins, structure determination.

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