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Volumn 113, Issue 36, 2009, Pages 12257-12264

Aggregation of transmembrane peptides studied by spin-label EPR

Author keywords

[No Author keywords available]

Indexed keywords

AGGREGATES; AMIDES; AMINES; ATOMIC FORCE MICROSCOPY; ATOMIC SPECTROSCOPY; BIOCHEMISTRY; CRYSTALLINE MATERIALS; ELECTRON RESONANCE; ELECTRON SPIN RESONANCE SPECTROSCOPY; FLUORESCENCE SPECTROSCOPY; GELATION; GELS; LIQUIDS; MEMBRANES; PARAMAGNETIC RESONANCE; PARAMAGNETISM; PHOSPHOLIPIDS; QUANTUM THEORY; SPIN DYNAMICS;

EID: 69949178792     PISSN: 15206106     EISSN: None     Source Type: Journal    
DOI: 10.1021/jp901371h     Document Type: Article
Times cited : (20)

References (22)
  • 2
    • 33746647787 scopus 로고    scopus 로고
    • Peptides in lipid bilayers: The power of simple models
    • DOI 10.1016/j.sbi.2006.06.007, PII S0959440X06001114
    • (2) Killian, J. A.; Nyholm, T. K. M. Peptides in lipid bilayers: the power of simple models. Curr. Opin. Struct. Biol. 2006, 16 (4), 473-479. (Pubitemid 44149068)
    • (2006) Current Opinion in Structural Biology , vol.16 , Issue.4 , pp. 473-479
    • Killian, J.A.1    Nyholm, T.K.2
  • 3
    • 37049023237 scopus 로고    scopus 로고
    • On the orientation of a designed transmembrane peptide: Toward the right tilt angle
    • Ozdirekcan, S.; Etchebest, C.; Killian, J. A.; Fuchs, P. F. J. On the orientation of a designed transmembrane peptide: Toward the right tilt angle. J. Am. Chem. Soc. 2007, 129 (49), 15174-15181.
    • (2007) J. Am. Chem. Soc. , vol.129 , Issue.49 , pp. 15174-15181
    • Ozdirekcan, S.1    Etchebest, C.2    Killian, J.A.3    Fuchs, P.F.J.4
  • 6
    • 18244390978 scopus 로고    scopus 로고
    • A ruler for determining the position of proteins in membranes
    • Nielsen, R. D.; Che, K. P.; Gelb, M. H.; Robinson, B. H. A ruler for determining the position of proteins in membranes. J. Am. Chem. Soc. 2005, 127 (17), 6430-6442.
    • (2005) J. Am. Chem. Soc. , vol.127 , Issue.17 , pp. 6430-6442
    • Nielsen, R.D.1    Che, K.P.2    Gelb, M.H.3    Robinson, B.H.4
  • 7
    • 0030029091 scopus 로고    scopus 로고
    • Induction of nonbilayer structures in diacylphosphatidylcholine model membranes by transmembrane alphahelical peptides: Importance of hydrophobic mismatch and proposed role of tryptophans
    • Killian, J. A.; Salemink, I.; dePlanque, M. R. R.; Lindblom, G.; Koeppe, R. E.; Greathouse, D. V. Induction of nonbilayer structures in diacylphosphatidylcholine model membranes by transmembrane alphahelical peptides: Importance of hydrophobic mismatch and proposed role of tryptophans. Biochemistry 1996, 35 (3), 1037-1045.
    • (1996) Biochemistry , vol.35 , Issue.3 , pp. 1037-1045
    • Killian, J.A.1    Salemink, I.2    Deplanque, M.R.R.3    Lindblom, G.4    Koeppe, R.E.5    Greathouse, D.V.6
  • 8
    • 0034673978 scopus 로고    scopus 로고
    • Visualization of highly ordered striated domains induced by transmembrane peptides in supported phosphatidylcholine bilayers
    • Rinia, H. A.; Kik, R. A.; Demel, R. A.; Snel, M. M. E.; Killian, J. A.; van der Eerden, J. P. J. M.; de Kruijff, B. Visualization of highly ordered striated domains induced by transmembrane peptides in supported phosphatidylcholine bilayers. Biochemistry 2000, 39 (19), 5852-5858.
    • (2000) Biochemistry , vol.39 , Issue.19 , pp. 5852-5858
    • Rinia, H.A.1    Kik, R.A.2    Demel, R.A.3    Snel, M.M.E.4    Killian, J.A.5    Van Der Eerden, J.P.J.M.6    De Kruijff, B.7
  • 9
    • 33645028968 scopus 로고    scopus 로고
    • Striated domains: Self-organizing ordered assemblies of transmembrane alpha-helical peptides and lipids in bilayers
    • de Kruijff, B.; Killian, J. A.; Ganchev, D. N.; Rinia, H. A.; Sparr, E. Striated domains: self-organizing ordered assemblies of transmembrane alpha-helical peptides and lipids in bilayers. Biol. Chem. 2006, 387 (3), 235-241.
    • (2006) Biol. Chem. , vol.387 , Issue.3 , pp. 235-241
    • De Kruijff, B.1    Killian, J.A.2    Ganchev, D.N.3    Rinia, H.A.4    Sparr, E.5
  • 10
    • 28244458040 scopus 로고    scopus 로고
    • Self-association of transmembrane alpha-helices in model membranes - Importance of helix orientation and role of hydrophobic mismatch
    • Sparr, E.; Ash, W. L.; Nazarov, P. V.; Rijkers, D. T. S.; Hemminga, M. A.; Tieleman, D. P.; Killian, J. A. Self-association of transmembrane alpha-helices in model membranes - Importance of helix orientation and role of hydrophobic mismatch. J. Biol. Chem 2005, 280 (47), 39324-39331.
    • (2005) J. Biol. Chem , vol.280 , Issue.47 , pp. 39324-39331
    • Sparr, E.1    Ash, W.L.2    Nazarov, P.V.3    Rijkers, D.T.S.4    Hemminga, M.A.5    Tieleman, D.P.6    Killian, J.A.7
  • 11
    • 0032581038 scopus 로고    scopus 로고
    • 2H NMR and ESR study using designed transmembrane α-helical peptides and gramicidin A
    • DOI 10.1021/bi980233r
    • (11) de Planque, M. R. R.; Greathouse, D. V.; Koeppe, R. E.; Schäfer, H.; Marsh, D.; Killian, J. A. Influence of lipid/peptide hydrophobic mismatch on the thickness of diacylphosphatidylcholine bilayers. A H-2 NMR and ESR study using designed transmembrane alpha-helical peptides and gramicidin A. Biochemistry 1998, 37 (26), 9333-9345. (Pubitemid 28307687)
    • (1998) Biochemistry , vol.37 , Issue.26 , pp. 9333-9345
    • De Planque, M.R.R.1    Greathouse, D.V.2    Koeppe II, R.E.3    Schafer, H.4    Marsh, D.5    Killian, J.A.6
  • 12
    • 0035061714 scopus 로고    scopus 로고
    • Constrained modeling of spin-labeled major coat protein mutants from M13 bacteriophage in a phospholipid bilayer
    • DOI 10.1110/ps.43801
    • (12) Bashtovyy, D.; Marsh, D.; Hemminga, M. A.; Pali, T. Constrained modeling of spin-labeled major coat protein mutants from M13 bacteriophage in a phospholipid bilayer. Protein Sci. 2001, 10 (5), 979-987. (Pubitemid 32367489)
    • (2001) Protein Science , vol.10 , Issue.5 , pp. 979-987
    • Bashtovyy, D.1    Marsh, D.2    Hemminga, M.A.3    Pali, T.4
  • 14
    • 0141733169 scopus 로고    scopus 로고
    • Structural organization of α-synuclein fibrils studied by site-directed spin labeling
    • DOI 10.1074/jbc.M305266200
    • (14) Der-Sarkissian, A.; Jao, C. C.; Chen, J.; Langen, R. Structural organization of alpha-synuclein fibrils studied by site-directed spin labeling. J. Biol. Chem. 2003, 278 (39), 37530-37535. (Pubitemid 37175274)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.39 , pp. 37530-37535
    • Der-Sarkissiant, A.1    Jao, C.C.2    Chen, J.3    Langen, R.4
  • 15
    • 33644849922 scopus 로고    scopus 로고
    • Measurement of thermodynamic parameters for hydrophobic mismatch 1: Self-association of a transmembrane helix
    • DOI 10.1021/bi0522854
    • (15) Yano, Y.; Matsuzaki, K. Measurement of thermodynamic parameters for hydrophobic mismatch 1: Self-association of a transmembrane helix. Biochemistry 2006, 45 (10), 3370-3378. (Pubitemid 43376355)
    • (2006) Biochemistry , vol.45 , Issue.10 , pp. 3370-3378
    • Yano, Y.1    Matsuzaki, K.2
  • 16
    • 28844486080 scopus 로고    scopus 로고
    • EasySpin, a comprehensive software package for spectral simulation and analysis in EPR
    • Stoll, S.; Schweiger, A. EasySpin, a comprehensive software package for spectral simulation and analysis in EPR. J. Magn. Reson. 2006, 178 (1), 42-55.
    • (2006) J. Magn. Reson. , vol.178 , Issue.1 , pp. 42-55
    • Stoll, S.1    Schweiger, A.2
  • 17
    • 20444460846 scopus 로고    scopus 로고
    • 1-ATP synthase from E. coli
    • DOI 10.1016/j.bbabio.2005.03.013, PII S0005272805000915
    • (17) Steigmiller, S.; Börsch, M.; Gräber, P.; Huber, M. Distances between the b-subunits in the tether domain of F0F1-ATP synthase from E. coli. Biochim. Biophys. Acta-Bioenerg. 2005, 1708 (2), 143-153. (Pubitemid 40824944)
    • (2005) Biochimica et Biophysica Acta - Bioenergetics , vol.1708 , Issue.2 , pp. 143-153
    • Steigmiller, S.1    Borsch, M.2    Graber, P.3    Huber, M.4
  • 18
    • 3142735737 scopus 로고    scopus 로고
    • Methods for study of protein dynamics and proteinprotein interaction in protein-ubiquitination by electron paramagnetic resonance spectroscopy
    • Steinhoff, H. J. Methods for study of protein dynamics and proteinprotein interaction in protein-ubiquitination by electron paramagnetic resonance spectroscopy. Frontiers Biosci. 2002, 7, C97-C110.
    • (2002) Frontiers Biosci. , vol.7
    • Steinhoff, H.J.1
  • 19
    • 0003765926 scopus 로고
    • John Wiley & Sons: New York
    • Lipid-Protein Interactions; John Wiley & Sons: New York, 1982.
    • (1982) Lipid-Protein Interactions
  • 22
    • 0020104545 scopus 로고
    • Interactions between Neutral Phospholipid-Bilayer Membranes
    • Lis, L. J.; Mcalister, M.; Fuller, N.; Rand, R. P.; Parsegian, V. A. Interactions Between Neutral Phospholipid-Bilayer Membranes. Biophys. J. 1982, 37 (3), 657-665.
    • (1982) Biophys. J. , vol.37 , Issue.3 , pp. 657-665
    • Lis, L.J.1    Mcalister, M.2    Fuller, N.3    Rand, R.P.4    Parsegian, V.A.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.