Home Full-length Vpu and human CD4(372–433) in phospholipid bilayers as seen by magic angle spinning NMR
Article
Licensed
Unlicensed Requires Authentication

Full-length Vpu and human CD4(372–433) in phospholipid bilayers as seen by magic angle spinning NMR

  • Hoa Q. Do , Marc Wittlich , Julian M. Glück , Luis Möckel , Dieter Willbold , Bernd W. Koenig and Henrike Heise EMAIL logo
Published/Copyright: July 16, 2013
Biological Chemistry
From the journal Biological Chemistry Volume 394 Issue 11

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 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.

Keywords: CD4; HIV-1 Vpu; lipid-edited solid-state NMR spectroscopy; POPC lipid bilayers
Corresponding author: Henrike Heise, Institute of Complex Systems (ICS-6), Research Center Jülich, D-52425 Jülich, Germany; and Institute of Physical Biology, Heinrich-Heine-University Düsseldorf, Universitätsstrasse 1, D-40225 Düsseldorf, Germany, e-mail:

We thank Sameer Singh for useful discussions and help with sample preparation. We gratefully acknowledge financial support and training from the International NRW Research School BioStruct, granted by the Ministry of Innovation, Science and Research of the State North Rhine-Westphalia, the Heinrich Heine University of Düsseldorf, and the Entrepreneur Foundation at the Heinrich Heine University of Düsseldorf.

References

Andrew, E.R., Bradbury, A., and Eades, R.G. (1958). Nuclear magnetic resonance spectra from a crystal rotated at high speed. Nature 182, 1659.10.1038/1821659a0Search in Google Scholar

Andronesi, O.C., Becker, S., Seidel, K., Heise, H., Young, H.S., and Baldus, M. (2005). Determination of membrane protein structure and dynamics by magic-angle-spinning solid-state NMR spectroscopy. J. Am. Chem. Soc. 127, 12965–12974.10.1021/ja0530164Search in Google Scholar

Bloembergen, N. (1949). On the interaction of nuclear spins in a crystalline lattice. Physica 15, 386–426.10.1016/0031-8914(49)90114-7Search in Google Scholar

Bour, S., Schubert, U., and Strebel, K. (1995). The human-immunodeficiency-virus type-1 Vpu protein secifically binds to the cytoplasmic domain of CD4 – implications for the mechanism of degradation. J. Virol. 69, 1510–1520.10.1128/jvi.69.3.1510-1520.1995Search in Google Scholar

Burum, D.P. and Ernst, R.R. (1980). Net polarization transfer via a J-ordered state for signal enhancement of low-sensitivity nuclei. J. Magn. Reson. 39, 163–168.10.1016/0022-2364(80)90168-7Search in Google Scholar

Chengmayer, C., Quiroga, M., Tung, J.W., Dina, D., and Levy, J.A. (1990). Viral determinants of human-immunodeficiency-virus type-1 T-cell or macrophage tropism, cytopathogenicity, and CD4 antigen modulation. J. Virol. 64, 4390–4398.10.1128/jvi.64.9.4390-4398.1990Search in Google Scholar

Cherry, R.J. (1975). Protein mobility in membranes. FEBS Lett. 55, 1–7.10.1016/0014-5793(75)80943-4Search in Google Scholar

Cohen, E.A., Terwilliger, E.F., Sodroski, J.G., and Haseltine, W.A. (1988). Identification of a protein encoded by the Vpu gene of HIV-1. Nature 334, 532–534.10.1038/334532a0Search in Google Scholar PubMed

Cook, G.A., Zhang, H., Park, S.H., Wang, Y., and Opella, S.J. (2011). Comparative NMR studies demonstrate profound differences between two viroporins: p7 of HCV and Vpu of HIV-1. Biochim. Biophys. Acta Biomembr. 1808, 554–560.10.1016/j.bbamem.2010.08.005Search in Google Scholar PubMed PubMed Central

Cordes, F.S., Tustian, A.D., Sansom, M.S.P., Watts, A., and Fischer, W.B. (2002). Bundles consisting of extended transmembrane segments of Vpu from HIV-1: computer simulations and conductance measurements. Biochemistry 41, 7359–7365.10.1021/bi025518pSearch in Google Scholar PubMed

De Angelis, A.A., Nevzorov, A.A., Park, S.H., Howell, S.C., Mrse, A.A., and Opella, S.J. (2004). High-resolution NMR spectroscopy of membrane proteins in aligned bicelles. J. Am. Chem. Soc. 126, 15340–15341.10.1021/ja045631ySearch in Google Scholar PubMed

Delaglio, F., Grzesiek, S., Vuister, G.W., Zhu, G., Pfeifer, J., and Bax, A. (1995). NMRPipe: a multidimensional spectral processing system based on UNIX pipes. J. Biomol. NMR 6, 277–293.10.1007/BF00197809Search in Google Scholar PubMed

Dube, M., Bego, M.G., Paquay, C., and Cohen, E.A. (2010). Modulation of HIV-1-host interaction: role of the Vpu accessory protein. Retrovirology 7, 114.10.1186/1742-4690-7-114Search in Google Scholar PubMed PubMed Central

Fares, C., Qian, J., and Davis, J.H. (2005). Magic angle spinning and static oriented sample NMR studies of the relaxation in the rotating frame of membrane peptides. J. Chem. Phys. 122, 194908–194917.10.1063/1.1899645Search in Google Scholar

Fischer, W.B., Wang, Y.-T., Schindler, C., and Chen, C.-P. (2012). Mechanism of function of viral channel proteins and implications for drug development. Int. Rev. Cell Mol. Biol. 294, 259–321.10.1016/B978-0-12-394305-7.00006-9Search in Google Scholar PubMed PubMed Central

Fung, B.M., Khitrin, A.K., and Ermolaev, K. (2000). An improved broadband decoupling sequence for liquid crystals and solids. J. Magn. Reson. 142, 97–101.10.1006/jmre.1999.1896Search in Google Scholar PubMed

Goddard, T.D. and Kneller, D.G. SPARKY 3. University of California, San Francisco, CA.Search in Google Scholar

Hartmann, S.R. and Hahn, E.L. (1962). Nuclear double resonance in rotating frame. Phys. Rev. 128, 2042–2053.10.1103/PhysRev.128.2042Search in Google Scholar

Heise, H., Köhler, F.H., and Xie, X.L. (2001). Solid-state NMR spectroscopy of paramagnetic metallocenes. J. Magn. Reson. 150, 198–206.10.1006/jmre.2001.2343Search in Google Scholar PubMed

Hohwy, M., Rienstra, C.M., Jaroniec, C.P., and Griffin, R.G. (1999). Fivefold symmetric homonuclear dipolar recoupling in rotating solids: application to double quantum spectroscopy. J. Chem. Phys. 110, 7983–7992.10.1063/1.478702Search in Google Scholar

Hong, M., Zhang, Y., and Hu, F.H. (2012). Membrane protein structure and dynamics from NMR spectroscopy. Annu. Rev. Phys. Chem. 63, 1–24.10.1146/annurev-physchem-032511-143731Search in Google Scholar PubMed PubMed Central

Huster, D., Yao, X.L., and Hong, M. (2002). Membrane protein topology probed by H-1 spin diffusion from lipids using solid-state NMR spectroscopy. J. Am. Chem. Soc. 124, 874–883.10.1021/ja017001rSearch in Google Scholar PubMed

Kijac, A., Shih, A.Y., Nieuwkoop, A.J., Schulten, K., Sligar, S.G., and Rienstra, C.M. (2010). Lipid-protein correlations in nanoscale phospholipid bilayers determined by solid-state nuclear magnetic resonance. Biochemistry 49, 9190–9198.10.1021/bi1013722Search in Google Scholar PubMed PubMed Central

Klimkait, T., Strebel, K., Hoggan, M.D., Martin, M.A., and Orenstein, J.M. (1990). The human immunodeficiency virus type 1-specific protein vpu is required for efficient virus maturation and release. J. Virol. 64, 621–629.10.1128/jvi.64.2.621-629.1990Search in Google Scholar

Kochendoerfer, G.G., Jones, D.H., Lee, S., Oblatt-Montal, M., Opella, S.J., and Montal, M. (2004). Functional characterization and NMR Spectroscopy on full-length Vpu from HIV-1 prepared by total chemical synthesis. J. Am. Chem. Soc. 126, 2439–2446.10.1021/ja038985iSearch in Google Scholar PubMed

Kumashiro, K.K., Schmidt-Rohr, K., Murphy, O.J., Ouellette, K.L., Cramer, W.A., and Thompson, L.K. (1998). A novel tool for probing membrane protein structure: solid-state NMR with proton spin diffusion and X-nucleus detection. J. Am. Chem. Soc. 120, 5043–5051.10.1021/ja972655eSearch in Google Scholar

Lenburg, M.E. and Landau, N.R. (1993). Vpu-induced degradation of CD4 – requirement for specific amino-acid-residues in the cytoplasmic domain of CD4. J. Virol. 67, 7238–7245.10.1128/jvi.67.12.7238-7245.1993Search in Google Scholar PubMed PubMed Central

Lewis, B.A., Harbison, G.S., Herzfeld, J., and Griffin, R.G. (1985). NMR structural-analysis of a membrane-protein-bacteriorhodopsin peptide backbone orientation and motion. Biochemistry 24, 4671–4679.10.1021/bi00338a029Search in Google Scholar PubMed

Litman, B.J., Lewis, E.N., and Levin, I.W. (1991). Packing characteristics of highly unsaturated bilayer lipids: Raman spectroscopic studies of multilamellar phosphatidylcholine dispersions. Biochemistry 30, 313–319.10.1021/bi00216a001Search in Google Scholar PubMed

Lowe, I.J. (1959). Free induction decays of rotating solids. Phys. Rev. Lett. 2, 285–287.10.1103/PhysRevLett.2.285Search in Google Scholar

Lu, J.X., Sharpe, S., Ghirlando, R., Yau, W.M., and Tycko, R. (2010). Oligomerization state and supramolecular structure of the HIV-1 Vpu protein transmembrane segment in phospholipid bilayers. Protein Sci. 19, 1877–1896.10.1002/pro.474Search in Google Scholar PubMed PubMed Central

Luca, S., Filippov, D.V., van Boom, J.H., Oschkinat, H., de Groot, H.J.M., and Baldus, M. (2001). Secondary chemical shifts in immobilized peptides and proteins: A qualitative basis for structure refinement under Magic Angle Spinning. J. Biomol. NMR 20, 325–331.10.1023/A:1011278317489Search in Google Scholar

Luis Nieva, J., Madan, V., and Carrasco, L. (2012). Viroporins: structure and biological functions. Nat Rev Microbiol 10, 563–574.10.1038/nrmicro2820Search in Google Scholar

Ma, C., Marassi, F.M., Jones, D.H., Straus, S.K., Bour, S., Strebel, K., Schubert, U., Oblatt-Montal, M., Montal, M., and Opella, S.J. (2002). Expression, purification, and activities of full-length and truncated versions of the integral membrane protein Vpu from HIV-1. Protein Sci. 11, 546–557.10.1110/ps.37302Search in Google Scholar

Maddon, P.J., Littman, D.R., Godfrey, M., Maddon, D.E., Chess, L., and Axel, R. (1985). The isolation and nucleotide-sequence of a cDNA encoding the T-cell surface protein T4 – a newer member of the immunoglobulin gene family. Cell 42, 93–104.10.1016/S0092-8674(85)80105-7Search in Google Scholar

Maddon, P.J., Molineaux, S.M., Maddon, D.E., Zimmerman, K.A., Godfrey, M., Alt, F.W., Chess, L., and Axel, R. (1987). Structure and expression of the human and mouse T4 genes. Proc. Natl. Acad. Sci. USA 84, 9155–9159.10.1073/pnas.84.24.9155Search in Google Scholar PubMed PubMed Central

Magadan, J.G. and Bonifacino, J.S. (2012). Transmembrane domain determinants of CD4 downregulation by HIV-1 Vpu. J. Virol. 86, 757–772.10.1128/JVI.05933-11Search in Google Scholar PubMed PubMed Central

Magadan, J.G., Perez-Victoria, F.J., Sougrat, R., Ye, Y., Strebel, K., and Bonifacino, J.S. (2010). Multilayered mechanism of CD4 downregulation by HIV-1 Vpu involving distinct ER retention and ERAD targeting steps. PLoS Pathog. 6, e1000869.10.1371/journal.ppat.1000869Search in Google Scholar PubMed PubMed Central

Maldarelli, F., Chen, M.Y., Willey, R.L., and Strebel, K. (1993). Human-immunodeficiency-virus type-1 Vpu protein is an oligomeric type-I integral membrane-protein. J. Virol. 67, 5056–5061.10.1128/jvi.67.8.5056-5061.1993Search in Google Scholar

Marassi, F.M., Das, B.B., Lu, G.J., Nothnagel, H.J., Park, S.H., Son, W.S., Tian, Y., and Opella, S.J. (2011). Structure determination of membrane proteins in five easy pieces. Methods 55, 363–369.10.1016/j.ymeth.2011.09.009Search in Google Scholar PubMed PubMed Central

Margottin, F., Benichou, S., Durand, H., Richard, V., Liu, L.X., Gomas, E., and Benarous, R. (1996). Interaction between the cytoplasmic domains of HIV-1 Vpu and CD4: role of Vpu residues involved in CD4 interaction and in vitro CD4 degradation. Virology 223, 381–386.10.1006/viro.1996.0491Search in Google Scholar PubMed

McDermott, A. (2009). Structure and dynamics of membrane proteins by magic angle spinning solid-state NMR. Annu. Rev. Biophys. 38, 385–403.10.1146/annurev.biophys.050708.133719Search in Google Scholar PubMed

Miao, Y., Qin, H., Fu, R., Sharma, M., Can, T.V., Hung, I., Luca, S., Gor’kov, P.L., Brey, W.W., and Cross, T.A. (2012). M2 proton channel structural validation from full-length protein samples in synthetic bilayers and E. coli membranes. Angew. Chem. Int. Ed. 51, 8383–8386.10.1002/anie.201204666Search in Google Scholar PubMed PubMed Central

Morris, G.A. and Freeman, R. (1979). Enhancement of nuclear magnetic-resonance signals by polarization transfer. J. Am. Chem. Soc. 101, 760–762.10.1021/ja00497a058Search in Google Scholar

Neil, S.J.D., Zang, T., and Bieniasz, P.D. (2008). Tetherin inhibits retrovirus release and is antagonized by HIV-1 Vpu. Nature 451, 425–U421.10.1038/nature06553Search in Google Scholar PubMed

Page, R.C., Li, C., Hu, J., Gao, F.P., and Cross, T.A. (2007). Lipid bilayers: an essential environment for the understanding of membrane proteins. Magn. Reson. Chem. 45, S2–S11.10.1002/mrc.2077Search in Google Scholar PubMed

Park, S.H. and Opella, S.J. (2005). Tilt angle of a trans-membrane helix is determined by hydrophobic mismatch. J. Mol. Biol. 350, 310–318.10.1016/j.jmb.2005.05.004Search in Google Scholar PubMed

Park, S.H. and Opella, S.J. (2007). Conformational changes induced by a single amino acid substitution in the trans-membrane domain of Vpu: Implications for HIV-1 susceptibility to channel blocking drugs. Protein Sci. 16, 2205–2215.10.1110/ps.073041107Search in Google Scholar PubMed PubMed Central

Park, S.H., Mrse, A.A., Nevzorov, A.A., Mesleh, M.F., Oblatt-Montal, M., Montal, M., and Opella, S.J. (2003). Three-dimensional structure of the channel-forming trans-membrane domain of virus protein "u" (Vpu) from HIV-1. J. Mol. Biol. 333, 409–424.10.1016/j.jmb.2003.08.048Search in Google Scholar PubMed

Park, S.H., De Angelis, A.A., Nevzorov, A.A., Wu, C.H., and Opella, S.J. (2006a). Three-dimensional structure of the transmembrane domain of Vpu from HIV-1 in aligned phospholipid bicelles. Biophys J. 91, 3032–3042.10.1529/biophysj.106.087106Search in Google Scholar PubMed PubMed Central

Park, S.H., Mrse, A.A., Nevzorov, A.A., De Angelis, A.A., and Opella, S.J. (2006b). Rotational diffusion of membrane proteins in aligned phospholipid bilayers by solid-state NMR spectroscopy. J. Magn. Reson. 178, 162–165.10.1016/j.jmr.2005.08.008Search in Google Scholar PubMed

Pines, A., Gibby, M.G., and Waugh, J.S. (1973). Proton-enhanced NMR of dilute spins in solids. J. Chem. Phys. 59, 569–590.10.1063/1.1680061Search in Google Scholar

Schubert, U., Bour, S., FerrerMontiel, A.V., Montal, M., Maldarelli, F., and Strebel, K. (1996a). The two biological activities of human immunodeficiency virus type 1 Vpu protein involve two separable structural domains. J. Virol. 70, 809–819.10.1128/jvi.70.2.809-819.1996Search in Google Scholar

Schubert, U., FerrerMontiel, A.V., OblattMontal, M., Henklein, P., Strebel, K., and Montal, M. (1996b). Identification of an ion channel activity of the Vpu transmembrane domain and its involvement in the regulation of virus release from HIV-1-infected cells. FEBS Lett. 398, 12–18.10.1016/S0014-5793(96)01146-5Search in Google Scholar

Seidel, K., Lange, A., Becker, S., Hughes, C.E., Heise, H., and Baldus, M. (2004). Protein solid-state NMR resonance assignments from (C-13, C-13) correlation spectroscopy. Phys. Chem. Chem. Phys. 6, 5090–5093.10.1039/b411689eSearch in Google Scholar

Sharpe, S., Yau, W.M., and Tycko, R. (2006). Structure and dynamics of the HIV-1 Vpu transmembrane domain revealed by solid-state NMR with magic-angle spinning. Biochemistry 45, 918–933.10.1021/bi051766kSearch in Google Scholar PubMed

Singh, S.K., Mockel, L., Thiagarajan-Rosenkranz, P., Wittlich, M., Willbold, D., and Koenig, B.W. (2012). Mapping the interaction between the cytoplasmic domains of HIV-1 viral protein U and human CD4 with NMR spectroscopy. FEBS J. 279, 3705–3714.10.1111/j.1742-4658.2012.08732.xSearch in Google Scholar PubMed

Strebel, K., Klimkait, T., and Martin, M.A. (1988). A novel gene of HIV-1, Vpu, and its 16-kilodalton product. Science 241, 1221–1223.10.1126/science.3261888Search in Google Scholar PubMed

Strebel, K., Klimkait, T., Maldarelli, F., and Martin, M.A. (1989). Molecular and biochemical analyses of human immunodeficiency virus type 1 vpu protein. J. Virol. 63, 3784–3791.10.1128/jvi.63.9.3784-3791.1989Search in Google Scholar PubMed PubMed Central

Szeverenyi, N.M., Sullivan, M.J., and Maciel, G.E. (1982). Observation of spin exchange by two-dimensional Fourier-transform C-13 cross polarization magic-angle spinning. J. Magn. Reson. 47, 462–475.Search in Google Scholar

Tiganos, E., Yao, X.J., Friborg, J., Daniel, N., and Cohen, E.A. (1997). Putative α-helical structures in the human immunodeficiency virus type 1 Vpu protein and CD4 are involved in binding and degradation of the CD4 molecule. J. Virol. 71, 4452–4460.10.1128/jvi.71.6.4452-4460.1997Search in Google Scholar

Van Damme, N., Goff, D., Katsura, C., Jorgenson, R.L., Mitchell, R., Johnson, M.C., Stephens, E.B., and Guatelli, J. (2008). The interferon-induced protein BST-2 restricts HIV-1 release and is downregulated from the cell surface by the viral Vpu protein. Cell Host Microbe 3, 245–252.10.1016/j.chom.2008.03.001Search in Google Scholar PubMed PubMed Central

Vincent, M.J., Raja, N.U., and Jabbar, M.A. (1993). Human-immunodeficiency-virus type-1 Vpu protein induces degradation of chimeric envelope glycoproteins bearing the cytoplasmic and anchor domains of CD4 – role of the cytoplasmic domain in Vpu-induced degradation in the endoplasmic-reticulum. J. Virol. 67, 5538–5549.10.1128/jvi.67.9.5538-5549.1993Search in Google Scholar PubMed PubMed Central

Wei, Y., Lee, D.-K., and Ramamoorthy, A. (2001). Solid-state 13C NMR chemical shift anisotropy tensors of polypeptides. J. Am. Chem. Soc. 123, 6118–6126.10.1021/ja010145lSearch in Google Scholar PubMed

Willey, R.L., Bucklerwhite, A., and Strebel, K. (1994). Sequences present in the cytoplasmic domain of CD4 are necessary and sufficient to confer sensitivity to the human-immunodeficiency-virus type-1 Vpu protein. J. Virol. 68, 1207–1212.10.1128/jvi.68.2.1207-1212.1994Search in Google Scholar

Wittlich, M., Koenig, B.W., Hoffmann, S., and Willbold, D. (2007a). Structural characterization of the transmembrane and cytoplasmic domains of human CD4. Biochim. Biophys. Acta Biomembr. 1768, 2949–2960.10.1016/j.bbamem.2007.10.023Search in Google Scholar PubMed

Wittlich, M., Wiesehan, K., Koenig, B.W., and Willbold, D. (2007b). Expression, purification, and membrane reconstitution of a CD4 fragment comprising the transmembrane and cytoplasmic domains of the receptor. Protein Expr. Purif. 55, 198–207.10.1016/j.pep.2007.05.007Search in Google Scholar PubMed

Wittlich, M., Koenig, B.W., Stoldt, M., Schmidt, H., and Willbold, D. (2009). NMR structural characterization of HIV-1 virus protein U cytoplasmic domain in the presence of dodecylphosphatidylcholine micelles. FEBS J. 276, 6560–6575.10.1111/j.1742-4658.2009.07363.xSearch in Google Scholar PubMed

Wittlich, M., Thiagarajan, P., Koenig, B.W., Hartmann, R., and Willbold, D. (2010). NMR structure of the transmembrane and cytoplasmic domains of human CD4 in micelles. Biochim. Biophys. Acta Biomembr. 1798, 122–127.10.1016/j.bbamem.2009.09.010Search in Google Scholar PubMed

Yang, J., Aslimovska, L., and Glaubitz, C. (2011). Molecular dynamics of proteorhodopsin in lipid bilayers by solid-state NMR. J. Am. Chem. Soc. 133, 4874–4881.10.1021/ja109766nSearch in Google Scholar PubMed

Yao, X.J., Friborg, J., Checroune, F., Gratton, S., Boisvert, F., Sekaly, R.P., and Cohen, E.A. (1995). Degradation of CD4 induced by human-immunodeficiency-virus type-1 Vpu protein – a predicted alpha-helix structure in the proximal cytoplasmic region of CD4 contributes to Vpu sensitivity. Virology 209, 615–623.10.1006/viro.1995.1293Search in Google Scholar PubMed

Received: 2013-5-28
Accepted: 2013-7-13
Published Online: 2013-07-16
Published in Print: 2013-11-01

©2013 by Walter de Gruyter Berlin Boston

Articles in the same Issue

  1. Masthead
  2. Masthead
  3. Guest Editorial
  4. Highlight: NRW Research School BioStruct – Biological Structures in Molecular Medicine and Biotechnology
  5. Highlight: NRW Research School Biostruct – Biological Structures in Molecular Medicine and Biotechnology
  6. Structural features of antiviral DNA cytidine deaminases
  7. Molecular insights into type I secretion systems
  8. Structural comparison of the transport units of type V secretion systems
  9. Rho-kinase: regulation, (dys)function, and inhibition
  10. Role of centrosomal adaptor proteins of the TACC family in the regulation of microtubule dynamics during mitotic cell division
  11. Revisiting Disrupted-in-Schizophrenia 1 as a scaffold protein
  12. Structural snapshot of cyclic nucleotide binding domains from cyclic nucleotide-sensitive ion channels
  13. Full-length Vpu and human CD4(372–433) in phospholipid bilayers as seen by magic angle spinning NMR
  14. Membrane protein stability depends on the concentration of compatible solutes – a single molecule force spectroscopic study
  15. Expression and characterisation of fully posttranslationally modified cellular prion protein in Pichia pastoris
  16. Contribution of distinct platelet integrins to binding, unfolding, and assembly of fibronectin
  17. Shear-related fibrillogenesis of fibronectin
  18. Enzyme-substrate complexes of the quinate/shikimate dehydrogenase from Corynebacterium glutamicum enable new insights in substrate and cofactor binding, specificity, and discrimination
  19. The amino acids surrounding the flavin 7a-methyl group determine the UVA spectral features of a LOV protein
  20. Determinants of the species selectivity of oxazolidinone antibiotics targeting the large ribosomal subunit
  21. NSR from Streptococcus agalactiae confers resistance against nisin and is encoded by a conserved nsr operon
https://doi.org/10.1515/hsz-2013-0194
Keywords for this article
CD4; HIV-1 Vpu; lipid-edited solid-state NMR spectroscopy; POPC lipid bilayers

Articles in the same Issue

  1. Masthead
  2. Masthead
  3. Guest Editorial
  4. Highlight: NRW Research School BioStruct – Biological Structures in Molecular Medicine and Biotechnology
  5. Highlight: NRW Research School Biostruct – Biological Structures in Molecular Medicine and Biotechnology
  6. Structural features of antiviral DNA cytidine deaminases
  7. Molecular insights into type I secretion systems
  8. Structural comparison of the transport units of type V secretion systems
  9. Rho-kinase: regulation, (dys)function, and inhibition
  10. Role of centrosomal adaptor proteins of the TACC family in the regulation of microtubule dynamics during mitotic cell division
  11. Revisiting Disrupted-in-Schizophrenia 1 as a scaffold protein
  12. Structural snapshot of cyclic nucleotide binding domains from cyclic nucleotide-sensitive ion channels
  13. Full-length Vpu and human CD4(372–433) in phospholipid bilayers as seen by magic angle spinning NMR
  14. Membrane protein stability depends on the concentration of compatible solutes – a single molecule force spectroscopic study
  15. Expression and characterisation of fully posttranslationally modified cellular prion protein in Pichia pastoris
  16. Contribution of distinct platelet integrins to binding, unfolding, and assembly of fibronectin
  17. Shear-related fibrillogenesis of fibronectin
  18. Enzyme-substrate complexes of the quinate/shikimate dehydrogenase from Corynebacterium glutamicum enable new insights in substrate and cofactor binding, specificity, and discrimination
  19. The amino acids surrounding the flavin 7a-methyl group determine the UVA spectral features of a LOV protein
  20. Determinants of the species selectivity of oxazolidinone antibiotics targeting the large ribosomal subunit
  21. NSR from Streptococcus agalactiae confers resistance against nisin and is encoded by a conserved nsr operon
Sign up now to receive a 20% welcome discount
Institutional Access
How does access work?
Have an idea on how to improve our website?
Please write us.
© 2025 De Gruyter Brill
Downloaded on 1.10.2025 from https://www.degruyterbrill.com/document/doi/10.1515/hsz-2013-0194/html?lang=en
Scroll to top button