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Refinement:
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Structure from chemical shifts:
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Secondary structure from chemical shifts:
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Flexibility from chemical shifts:
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Disordered proteins:
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Old 11-18-2010, 09:15 PM
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Default Three-dimensional solid-state NMR spectroscopy is essential for resolution of resonan

Three-dimensional solid-state NMR spectroscopy is essential for resolution of resonances from in-plane residues in uniformly (15)N-labeled helical membrane proteins in oriented lipid bilayers.

Related Articles Three-dimensional solid-state NMR spectroscopy is essential for resolution of resonances from in-plane residues in uniformly (15)N-labeled helical membrane proteins in oriented lipid bilayers.

J Magn Reson. 2000 May;144(1):156-61

Authors: Marassi FM, Ma C, Gesell JJ, Opella SJ

Uniformly (15)N-labeled samples of membrane proteins with helices aligned parallel to the membrane surface give two-dimensional PISEMA spectra that are highly overlapped due to limited dispersions of (1)H-(15)N dipolar coupling and (15)N chemical shift frequencies. However, resolution is greatly improved in three-dimensional (1)H chemical shift/(1)H-(15)N dipolar coupling/(15)N chemical shift correlation spectra. The 23-residue antibiotic peptide magainin and a 54-residue polypeptide corresponding to the cytoplasmic domain of the HIV-1 accessory protein Vpu are used as examples. Both polypeptides consist almost entirely of alpha-helices, with their axes aligned parallel to the membrane surface. The measurement of three orientationally dependent frequencies for Val17 of magainin enabled the three-dimensional orientation of this helical peptide to be determined in the lipid bilayer.

PMID: 10783286 [PubMed - indexed for MEDLINE]



Source: PubMed
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