TY  - JOUR
AU  - Do, Quynh Hoa
AU  - Wittlich, Marc
AU  - Glück, Julian
AU  - Möckel, Luis
AU  - Willbold, Dieter
AU  - König, Bernd
AU  - Heise, Henrike
TI  - Full-length Vpu and human CD4(372–433) in phospholipid bilayers as seen by magic angle spinning NMR
JO  - Biological chemistry
VL  - 394
IS  - 11
SN  - 1437-4315
CY  - Berlin [u.a.]
PB  - de Gruyter
M1  - FZJ-2013-05758
SP  - 1453 - 1463
PY  - 2013
AB  - 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 and 15N isotopes, and separately reconstituted into phospholipid bilayers. Highly resolved dipolar cross-polarization (CP)-based solid-state NMR spectra of the two transmembrane proteins were recorded under magic angle sample spinning. 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 transmembrane domains into the lipid bilayers was confirmed by proton spin diffusion experiments.
LB  - PUB:(DE-HGF)16
UR  - <Go to ISI:>//WOS:000325717100009
DO  - DOI:10.1515/hsz-2013-0194
UR  - https://juser.fz-juelich.de/record/139786
ER  -