ChemInform Abstract: Structure and Orientation of Ligands Bound to Membrane Proteins Are Reflected by Residual Dipolar Couplings in Solution NMR Measurements

ChemInform ◽  
2010 ◽  
Vol 33 (49) ◽  
pp. no-no
Author(s):  
Bernd W. Koenig
Keyword(s):  
Membrane Proteins ◽  
Residual Dipolar Couplings ◽  
Dipolar Couplings ◽  
Solution Nmr ◽  
Abstract Structure

Detecting Protein Kinase Recognition Modes of Calmodulin by Residual Dipolar Couplings in Solution NMR†

Biochemistry ◽  
2002 ◽  
Vol 41 (43) ◽  
pp. 12899-12906 ◽  
Author(s):  
Tapas K. Mal ◽  
Nikolai R. Skrynnikov ◽  
Kyoko L. Yap ◽  
Lewis E. Kay ◽  
Mitsuhiko Ikura
Keyword(s):  
Protein Kinase ◽  
Residual Dipolar Couplings ◽  
Dipolar Couplings ◽  
Solution Nmr

scholarly journals Solution NMR Experiment for Measurement of 15N–1H Residual Dipolar Couplings in Large Proteins and Supramolecular Complexes

2015 ◽  
Vol 137 (35) ◽  
pp. 11242-11245 ◽  
Author(s):  
Alexander Eletsky ◽  
Surya V.S.R.K. Pulavarti ◽  
Victor Beaumont ◽  
Paul Gollnick ◽  
Thomas Szyperski
Keyword(s):  
Residual Dipolar Couplings ◽  
Dipolar Couplings ◽  
Solution Nmr ◽  
Supramolecular Complexes ◽  
Large Proteins

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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