Dipolar Assisted Assignment Protocol (DAAP) for MAS solid-state NMR of rotationally aligned membrane proteins in phospholipid bilayers.

 In
by Bibhuti B Das, Hua Zhang, Stanley J Opella
Abstract:
A method for making resonance assignments in magic angle spinning solid-state NMR spectra of membrane proteins that utilizes the range of heteronuclear dipolar coupling frequencies in combination with conventional chemical shift based assignment methods is demonstrated. The Dipolar Assisted Assignment Protocol (DAAP) takes advantage of the rotational alignment of the membrane proteins in liquid crystalline phospholipid bilayers. Improved resolution is obtained by combining the magnetically inequivalent heteronuclear dipolar frequencies with isotropic chemical shift frequencies. Spectra with both dipolar and chemical shift frequency axes assist with resonance assignments. DAAP can be readily extended to three- and four-dimensional experiments and to include both backbone and side chain sites in proteins.
Reference:
Dipolar Assisted Assignment Protocol (DAAP) for MAS solid-state NMR of rotationally aligned membrane proteins in phospholipid bilayers. (Bibhuti B Das, Hua Zhang, Stanley J Opella), In Journal of magnetic resonance (San Diego, Calif. : 1997), volume 242, 2014.
Bibtex Entry:
@article{Das2014a,
abstract = {A method for making resonance assignments in magic angle spinning solid-state NMR spectra of membrane proteins that utilizes the range of heteronuclear dipolar coupling frequencies in combination with conventional chemical shift based assignment methods is demonstrated. The Dipolar Assisted Assignment Protocol (DAAP) takes advantage of the rotational alignment of the membrane proteins in liquid crystalline phospholipid bilayers. Improved resolution is obtained by combining the magnetically inequivalent heteronuclear dipolar frequencies with isotropic chemical shift frequencies. Spectra with both dipolar and chemical shift frequency axes assist with resonance assignments. DAAP can be readily extended to three- and four-dimensional experiments and to include both backbone and side chain sites in proteins.},
author = {Das, Bibhuti B and Zhang, Hua and Opella, Stanley J},
doi = {10.1016/j.jmr.2014.02.018},
issn = {1096-0856},
journal = {Journal of magnetic resonance (San Diego, Calif. : 1997)},
keywords = {MAS,Membrane protein,Solid state NMR,Vpu},
month = {may},
pages = {224--32},
pmid = {24698983},
title = {{Dipolar Assisted Assignment Protocol (DAAP) for MAS solid-state NMR of rotationally aligned membrane proteins in phospholipid bilayers.}},
url = {http://linkinghub.elsevier.com/retrieve/pii/S1090780714000561 http://www.ncbi.nlm.nih.gov/pubmed/24698983 http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=PMC4043445},
volume = {242},
year = {2014}
}

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