메뉴 건너뛰기




Volumn 94, Issue 11, 2008, Pages 4339-4347

Fluid mechanical matching of H+-ATP synthase subunit c-ring with lipid membranes revealed by2H solid-state NMR

Author keywords

[No Author keywords available]

Indexed keywords

DEUTERIUM; MOLECULAR MOTOR; PROTEIN SUBUNIT; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATASE;

EID: 44849115352     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1529/biophysj.107.123745     Document Type: Article
Times cited : (15)

References (41)
  • 1
    • 0031008228 scopus 로고    scopus 로고
    • The ATP synthase-a splendid molecular machine
    • Boyer, P. D. 1997. The ATP synthase-a splendid molecular machine. Annu. Rev. Biochem. 66:717-749.
    • (1997) Annu. Rev. Biochem , vol.66 , pp. 717-749
    • Boyer, P.D.1
  • 4
    • 0035942281 scopus 로고    scopus 로고
    • The preferred stoichiometry of c subunits in the rotary motor sector of Escherichia coli ATP synthase is 10
    • Jiang, W., J. Hermolin, and R. H. Fillingame. 2001. The preferred stoichiometry of c subunits in the rotary motor sector of Escherichia coli ATP synthase is 10. Proc. Natl. Acad. Sci. USA. 98:4966-4971.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 4966-4971
    • Jiang, W.1    Hermolin, J.2    Fillingame, R.H.3
  • 10
    • 0033581879 scopus 로고    scopus 로고
    • Structural changes linked to proton translocation by subunit c of the ATP synthase
    • Rastogi, V. K., and M. E. Girvin. 1999. Structural changes linked to proton translocation by subunit c of the ATP synthase. Nature. 402:263-268.
    • (1999) Nature , vol.402 , pp. 263-268
    • Rastogi, V.K.1    Girvin, M.E.2
  • 12
    • 17844392351 scopus 로고    scopus 로고
    • Nature's rotary electromotors
    • Junge, W., and N. Nelson. 2005. Nature's rotary electromotors. Science. 308:642-644.
    • (2005) Science , vol.308 , pp. 642-644
    • Junge, W.1    Nelson, N.2
  • 14
    • 0027483741 scopus 로고
    • 1H NMR resonance assignments and NOE analysis
    • 1H NMR resonance assignments and NOE analysis. Biochemistry. 32:12167-12177.
    • (1993) Biochemistry , vol.32 , pp. 12167-12177
    • Girvin, M.E.1    Fillingame, R.H.2
  • 16
    • 0346213760 scopus 로고
    • Direct determination of the oriented sample NMR spectrum from the powder spectrum for systems with local axial symmetry
    • Bloom, M., J. H. Davis, and A. L. MacKay. 1981. Direct determination of the oriented sample NMR spectrum from the powder spectrum for systems with local axial symmetry. Chem. Phys. Lett. 80:198-202.
    • (1981) Chem. Phys. Lett , vol.80 , pp. 198-202
    • Bloom, M.1    Davis, J.H.2    MacKay, A.L.3
  • 17
    • 0002737381 scopus 로고
    • Fast-Fourier-transform dePaking
    • McCabe, M. A., and S. R. Wassall. 1995. Fast-Fourier-transform dePaking. J. Magn. Reson. B. 106:80-82.
    • (1995) J. Magn. Reson. B , vol.106 , pp. 80-82
    • McCabe, M.A.1    Wassall, S.R.2
  • 19
    • 0000483987 scopus 로고    scopus 로고
    • Membrane structure and dynamics studied with NMR spectroscopy
    • Membranes. K. M. Merz Jr. and B. Roux, editors. Birkhauser, Boston, MA
    • Brown, M. F. 1996. Membrane structure and dynamics studied with NMR spectroscopy. In Biological Membranes. K. M. Merz Jr. and B. Roux, editors. Birkhauser, Boston, MA. 175-252.
    • (1996) Biological , pp. 175-252
    • Brown, M.F.1
  • 22
    • 0000354184 scopus 로고
    • Deuterium NMR study of intermolecular interactions in lamellar phases containing palmitoyllysophosphatidylcholine
    • Jansson, M., R. L. Thurmond, J. A. Barry, and M. F. Brown. 1992. Deuterium NMR study of intermolecular interactions in lamellar phases containing palmitoyllysophosphatidylcholine. J. Phys. Chem. 96:9532-9544.
    • (1992) J. Phys. Chem , vol.96 , pp. 9532-9544
    • Jansson, M.1    Thurmond, R.L.2    Barry, J.A.3    Brown, M.F.4
  • 23
    • 3142543171 scopus 로고    scopus 로고
    • Perturbation of the hydrophobic core of lipid bilayers by the human antimicrobial peptide LL-37
    • Henzler-Wildman, K. A., G. V. Martinez, M. F. Brown, and A. Ramamoorthy. 2004. Perturbation of the hydrophobic core of lipid bilayers by the human antimicrobial peptide LL-37. Biochemistry. 43:8459-8469.
    • (2004) Biochemistry , vol.43 , pp. 8459-8469
    • Henzler-Wildman, K.A.1    Martinez, G.V.2    Brown, M.F.3    Ramamoorthy, A.4
  • 24
    • 24644498037 scopus 로고    scopus 로고
    • Lipid modifications of a Ras peptide exhibit altered packing and mobility versus host membrane as detected by 2H solid-state NMR
    • Vogel, A., C. P. Katzka, H. Waldmann, K. Arnold, M. F. Brown, and D. Huster. 2005. Lipid modifications of a Ras peptide exhibit altered packing and mobility versus host membrane as detected by 2H solid-state NMR. J. Am. Chem. Soc. 127:12263-12272.
    • (2005) J. Am. Chem. Soc , vol.127 , pp. 12263-12272
    • Vogel, A.1    Katzka, C.P.2    Waldmann, H.3    Arnold, K.4    Brown, M.F.5    Huster, D.6
  • 25
    • 0025272761 scopus 로고
    • Purification of octyl β-D-glucopyranoside and re-estimation of its micellar size
    • Lorber, B., J. B. Bishop, and L. J. DeLukas. 1990. Purification of octyl β-D-glucopyranoside and re-estimation of its micellar size. Biochim. Biophys. Acta. 1023:254-265.
    • (1990) Biochim. Biophys. Acta , vol.1023 , pp. 254-265
    • Lorber, B.1    Bishop, J.B.2    DeLukas, L.J.3
  • 26
    • 0034707086 scopus 로고    scopus 로고
    • Interaction of membrane proteins and lipids with solubilizing detergents
    • le Maire, M., P. Champeil, and J. V. Moller. 2000. Interaction of membrane proteins and lipids with solubilizing detergents. Biochim. Biophys. Acta. 1508:86-111.
    • (2000) Biochim. Biophys. Acta , vol.1508 , pp. 86-111
    • le Maire, M.1    Champeil, P.2    Moller, J.V.3
  • 27
    • 0037181463 scopus 로고    scopus 로고
    • Self-assembly of ATP synthase subunit c rings
    • Arechaga, I., P. J. G. Butler, and J. E. Walker. 2002. Self-assembly of ATP synthase subunit c rings. FEBS Lett. 515:189-193.
    • (2002) FEBS Lett , vol.515 , pp. 189-193
    • Arechaga, I.1    Butler, P.J.G.2    Walker, J.E.3
  • 28
    • 0037064219 scopus 로고    scopus 로고
    • +-transporting ATP synthase derived by solution NMR and intersubunit cross-linking in situ
    • +-transporting ATP synthase derived by solution NMR and intersubunit cross-linking in situ. Biochim. Biophys. Acta. 1565:232-245.
    • (2002) Biochim. Biophys. Acta , vol.1565 , pp. 232-245
    • Fillingame, R.H.1    Dmitriev, O.Y.2
  • 30
    • 0000902639 scopus 로고    scopus 로고
    • Influence of cholesterol on dynamics of dimyristoyl- phosphatidylcholine bilayers as studied by deuterium NMR relaxation
    • Trouard, T. P., A. A. Nevzorov, T. M. Alam, C. Job, J. Zajicek, and M. F. Brown. 1999. Influence of cholesterol on dynamics of dimyristoyl- phosphatidylcholine bilayers as studied by deuterium NMR relaxation. J. Chem. Phys. 110:8802-8818.
    • (1999) J. Chem. Phys , vol.110 , pp. 8802-8818
    • Trouard, T.P.1    Nevzorov, A.A.2    Alam, T.M.3    Job, C.4    Zajicek, J.5    Brown, M.F.6
  • 31
    • 85031364904 scopus 로고    scopus 로고
    • Reference deleted in proof
    • Reference deleted in proof.
  • 32
    • 0021111152 scopus 로고
    • Membrane thickness and acyl chain length
    • Cornell, B. A., and F. Separovic. 1983. Membrane thickness and acyl chain length. Biochim. Biophys. Acta. 733:189-193.
    • (1983) Biochim. Biophys. Acta , vol.733 , pp. 189-193
    • Cornell, B.A.1    Separovic, F.2
  • 33
    • 1942519744 scopus 로고    scopus 로고
    • Membrane model for the G-protein-coupled receptor rhodopsin: Hydrophobic interface and dynamical structure
    • Huber, T., A. V. Botelho, K. Beyer, and M. F. Brown. 2004. Membrane model for the G-protein-coupled receptor rhodopsin: hydrophobic interface and dynamical structure. Biophys. J. 86:2078-2100.
    • (2004) Biophys. J , vol.86 , pp. 2078-2100
    • Huber, T.1    Botelho, A.V.2    Beyer, K.3    Brown, M.F.4
  • 34
    • 0029738872 scopus 로고    scopus 로고
    • Experimentally determined hydrophobicity scale for proteins at membrane interfaces
    • Wimly, W. C., and S. H. White. 1996. Experimentally determined hydrophobicity scale for proteins at membrane interfaces. Nat. Struct. Biol. 3:842-848.
    • (1996) Nat. Struct. Biol , vol.3 , pp. 842-848
    • Wimly, W.C.1    White, S.H.2
  • 35
    • 0345492016 scopus 로고    scopus 로고
    • Lipid-protein interactions studied by introduction of a tryptophan residue: The mechanosensitive channel MscL
    • Powl, A. M., J. M. East, and A. G. Lee. 2003. Lipid-protein interactions studied by introduction of a tryptophan residue: the mechanosensitive channel MscL. Biochemistry. 42:14306-14317.
    • (2003) Biochemistry , vol.42 , pp. 14306-14317
    • Powl, A.M.1    East, J.M.2    Lee, A.G.3
  • 36
    • 17144391476 scopus 로고    scopus 로고
    • Identification of the hydrophobic thickness of a membrane protein using fluorescence spectroscopy: Studies with the mechanosensitive channel MscL
    • Powl, A. M., J. N. Wright, J. M. East, and A. G. Lee. 2005. Identification of the hydrophobic thickness of a membrane protein using fluorescence spectroscopy: studies with the mechanosensitive channel MscL. Biochemistry. 44:5713-5721.
    • (2005) Biochemistry , vol.44 , pp. 5713-5721
    • Powl, A.M.1    Wright, J.N.2    East, J.M.3    Lee, A.G.4
  • 37
    • 0037125502 scopus 로고    scopus 로고
    • Elastic deformation of membrane bilayers probed by deuterium NMR relaxation
    • Brown, M. F., R. L. Thurmond, S. W. Dodd, D. Otten, and K. Beyer. 2002. Elastic deformation of membrane bilayers probed by deuterium NMR relaxation. J. Am. Chem. Soc. 124:8471-8484.
    • (2002) J. Am. Chem. Soc , vol.124 , pp. 8471-8484
    • Brown, M.F.1    Thurmond, R.L.2    Dodd, S.W.3    Otten, D.4    Beyer, K.5
  • 39
    • 0034499164 scopus 로고    scopus 로고
    • Softening of membrane bilayers by detergents elucidated by deuterium NMR spectroscopy
    • Otten, D., M. F. Brown, and K. Beyer. 2000. Softening of membrane bilayers by detergents elucidated by deuterium NMR spectroscopy. J. Phys. Chem. B. 104:12119-12129.
    • (2000) J. Phys. Chem. B , vol.104 , pp. 12119-12129
    • Otten, D.1    Brown, M.F.2    Beyer, K.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.