Related ArticlesFull-length Vpu and human CD4(372-433) in phospholipid bilayers as seen by magic angle spinning NMR.
Biol Chem. 2013 Jul 17;
Authors: Do HQ, Wittlich M, Glück JM, Möckel L, Willbold D, Koenig BW, Heise H
Abstract
Abstract HIV-1 Vpu and CD4(372-433), a peptide comprising the transmembrane and cytoplasmic domain of human CD4, were recombinantly expressed in Escherichia coli, uniformly labeled with 13C und 15N isotopes, and separately reconstituted into phospholipid bilayers. Highly resolved, dipolar cross polarization-based solid-state NMR spectra of the two transmembrane proteins were recorded under magic angle sample spinning (MAS). Partial assignment of 13C resonances was achieved. Site-specific assignments were obtained for 13 amino acid residues of CD4(372-433) and two VpU residues. Additional amino acid type-specific assignments were achieved for 10 amino acid spin systems for both CD4(372-433) and Vpu. Further, structural flexibility was probed with different dipolar recoupling techniques, and the correct insertion of the TM domains into the lipid bilayers was confirmed by proton spin diffusion experiments.
PMID: 23863698 [PubMed - as supplied by publisher]
[NMR paper] Magic Angle Spinning NMR of Paramagnetic Proteins.
Magic Angle Spinning NMR of Paramagnetic Proteins.
Related Articles Magic Angle Spinning NMR of Paramagnetic Proteins.
Acc Chem Res. 2013 Mar 18;
Authors: Knight MJ, Felli IC, Pierattelli R, Emsley L, Pintacuda G
Abstract
Metal ions are ubiquitous in biochemical and cellular processes. Since many metal ions are paramagnetic due to the presence of unpaired electrons, paramagnetic molecules are an important class of targets for research in structural biology and related fields. Today, NMR spectroscopy plays a central role in the...
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[NMR paper] Magic-Angle Spinning NMR of Cold Samples.
Magic-Angle Spinning NMR of Cold Samples.
Related Articles Magic-Angle Spinning NMR of Cold Samples.
Acc Chem Res. 2013 Mar 14;
Authors: Concistrè M, Johannessen OG, Carignani E, Geppi M, Levitt MH
Abstract
Magic-angle-spinning solid-state NMR provides site-resolved structural and chemical information about molecules that complements many other physical techniques. Recent technical advances have made it possible to perform magic-angle-spinning NMR experiments at low temperatures, allowing researchers to trap reaction intermediates and to...
[NMR paper] Mapping the binding site of full length HIV-1 Nef on human Lck SH3 by NMR spectroscop
Mapping the binding site of full length HIV-1 Nef on human Lck SH3 by NMR spectroscopy.
Related Articles Mapping the binding site of full length HIV-1 Nef on human Lck SH3 by NMR spectroscopy.
J Biomed Sci. 2005;12(3):451-6
Authors: Briese L, Preusser A, Willbold D
The Nef protein of human immunodeficiency virus type 1 (HIV-1) is known to directly bind to the SH3 domain of human lymphocyte specific kinase (Lck) via a proline-rich region located in the amino terminal part of Nef. To address the question whether Nef binding to Lck SH3 involves...
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[NMR paper] 13C magic angle spinning NMR characterization of the functionally asymmetric QA bindi
13C magic angle spinning NMR characterization of the functionally asymmetric QA binding in Rhodobacter sphaeroides R26 photosynthetic reaction centers using site-specific 13C-labeled ubiquinone-10.
Related Articles 13C magic angle spinning NMR characterization of the functionally asymmetric QA binding in Rhodobacter sphaeroides R26 photosynthetic reaction centers using site-specific 13C-labeled ubiquinone-10.
Biochemistry. 1995 Aug 15;34(32):10229-36
Authors: van Liemt WB, Boender GJ, Gast P, Hoff AJ, Lugtenburg J, de Groot HJ
Photosynthetic...
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[NMR paper] 13C magic angle spinning NMR evidence for a 15,15'-cis configuration of the spheroide
13C magic angle spinning NMR evidence for a 15,15'-cis configuration of the spheroidene in the Rhodobacter sphaeroides photosynthetic reaction center.
Related Articles 13C magic angle spinning NMR evidence for a 15,15'-cis configuration of the spheroidene in the Rhodobacter sphaeroides photosynthetic reaction center.
Biochemistry. 1992 Dec 15;31(49):12446-50
Authors: de Groot HJ, Gebhard R, van der Hoef I, Hoff AJ, Lugtenburg J, Violette CA, Frank HA
The photosynthetic reaction center of Rhodobacter sphaeroides 2.4.1 contains one carotenoid...
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[NMR paper] Cytochrome c interactions with cardiolipin in bilayers: a multinuclear magic-angle sp
Cytochrome c interactions with cardiolipin in bilayers: a multinuclear magic-angle spinning NMR study.
Related Articles Cytochrome c interactions with cardiolipin in bilayers: a multinuclear magic-angle spinning NMR study.
Biochemistry. 1992 Oct 20;31(41):10129-38
Authors: Spooner PJ, Watts A
The influence of cytochrome c binding to cardiolipin bilayers on the motional characteristics of each component has been analyzed by magic-angle spinning (MAS) NMR. Observations were made by NMR of natural abundance 31P, 13C, and 1H nuclei in the lipid as...
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[NMR paper] 13C magic-angle spinning NMR studies of bathorhodopsin, the primary photoproduct of r
13C magic-angle spinning NMR studies of bathorhodopsin, the primary photoproduct of rhodopsin.
Related Articles 13C magic-angle spinning NMR studies of bathorhodopsin, the primary photoproduct of rhodopsin.
Biochemistry. 1991 Jul 30;30(30):7409-15
Authors: Smith SO, Courtin J, de Groot H, Gebhard R, Lugtenburg J
Magic-angle spinning NMR spectra have been obtained of the bathorhodopsin photointermediate trapped at low temperature (less than 130 K) by using isorhodopsin samples regenerated with retinal specifically 13C-labeled at positions 8,...