ChemInform Abstract: CHEMICAL SHIFT CORRELATED TWO-DIMENSIONAL NMR SPECTROSCOPY AND ITS APPLICATION TO SOLVING THE PROTON NMR SPECTRA OF OLIGORIBONUCLEOTIDES

1981 ◽  
Vol 12 (1) ◽  
Author(s):  
A. D. BAIN ◽  
R. A. BELL ◽  
J. R. EVERETT ◽  
D. W. HUGHES
Keyword(s):  
Nmr Spectroscopy ◽  
Chemical Shift ◽  
Nmr Spectra ◽  
Proton Nmr ◽  
Two Dimensional

Chemical shift correlated two-dimensional nmr spectroscopy and its application to solving the proton nmr spectra of oligoribonucleotides

1980 ◽  
Vol 58 (18) ◽  
pp. 1947-1956 ◽  
Author(s):  
Alex D. Bain ◽  
Russell A. Bell ◽  
Jeremy R. Everett ◽  
Donald W. Hughes
Keyword(s):  
Nmr Spectroscopy ◽  
Chemical Shift ◽  
Nmr Spectra ◽  
Pulse Sequence ◽  
Chemical Shifts ◽  
Proton Nmr ◽  
Two Dimensional

An alternative two-dimensional nmr pulse sequence, (90°–t1/2–90°–t1/2–FID),correlates the chemical shifts of coupled nuclei. The application of this technique to the solution of the complicated proton nmr spectra of oligoribonucleotides is discussed.

Sequential resonance assignments in proton NMR spectra of oligonucleotides by two-dimensional NMR spectroscopy

Biochemistry ◽  
1984 ◽  
Vol 23 (7) ◽  
pp. 1371-1376 ◽  
Author(s):  
R. M. Scheek ◽  
R. Boelens ◽  
N. Russo ◽  
J. H. Van Boom ◽  
R. Kaptein
Keyword(s):  
Nmr Spectroscopy ◽  
Nmr Spectra ◽  
Proton Nmr ◽  
Resonance Assignments ◽  
Two Dimensional

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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