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Volumn 1063, Issue , 2013, Pages 95-116

Analyzing the effects of hydrophobic mismatch on transmembrane α-helices using tryptophan fluorescence spectroscopy

(1)  Caputo, Gregory A a  

a NONE

Author keywords

Fluorescence quenching; Fluorescence spectroscopy; Hydrophobic mismatch; Peptide design; Transmembrane helices

Indexed keywords

MEMBRANE PROTEIN; TRYPTOPHAN;

EID: 84934438684     PISSN: 10643745     EISSN: None     Source Type: Book Series    
DOI: 10.1007/978-1-62703-583-5_5     Document Type: Article
Times cited : (6)

References (108)
  • 1
    • 77949732088 scopus 로고    scopus 로고
    • Prediction of the human membrane proteome
    • doi: 10.1002/pmic.200900258
    • Fagerberg L, Jonasson K, von Heijne G, Uhlen M, Berglund L (2010) Prediction of the human membrane proteome. Proteomics 10 (6): 1141-1149. doi: 10.1002/pmic.200900258
    • (2010) Proteomics , vol.10 , Issue.6 , pp. 1141-1149
    • Fagerberg, L.1    Jonasson, K.2    Von Heijne, G.3    Uhlen, M.4    Berglund, L.5
  • 2
    • 79959429680 scopus 로고    scopus 로고
    • Transmembrane communication: General principles and lessons from the structure and function of the M2 proton channel, K (+) channels, and integrin receptors
    • doi: 10.1146/ annurev-biochem-091008-152423
    • Grigoryan G, Moore DT, DeGrado WF (2011) Transmembrane communication: general principles and lessons from the structure and function of the M2 proton channel, K (+) channels, and integrin receptors. Annu Rev Biochem 80:211-237. doi: 10.1146/ annurev-biochem-091008-152423
    • (2011) Annu Rev Biochem , vol.80 , pp. 211-237
    • Grigoryan, G.1    Moore, D.T.2    Degrado, W.F.3
  • 3
    • 84855782874 scopus 로고    scopus 로고
    • Computational design of membrane proteins
    • doi: 10.1016/j. str.2011.12.003
    • Perez-Aguilar JM, Saven JG (2012) Computational design of membrane proteins. Structure 20 (1):5-14. doi: 10.1016/j. str.2011.12.003
    • (2012) Structure , vol.20 , Issue.1 , pp. 5-14
    • Perez-Aguilar, J.M.1    Saven, J.G.2
  • 4
    • 4143085058 scopus 로고    scopus 로고
    • Folding of helical membrane proteins: The role of polar, GxxxG-like and proline motifs
    • doi: 10.1016/j.sbi.2004.07.007
    • Senes A, Engel DE, DeGrado WF (2004) Folding of helical membrane proteins: the role of polar, GxxxG-like and proline motifs. Curr Opin Struct Biol 14 (4):465-479. doi: 10.1016/j.sbi.2004.07.007
    • (2004) Curr Opin Struct Biol , vol.14 , Issue.4 , pp. 465-479
    • Senes, A.1    Engel, D.E.2    Degrado, W.F.3
  • 5
    • 54749145468 scopus 로고    scopus 로고
    • Peptide probes for protein transmembrane domains
    • doi: 10.1021/cb800049w
    • Slivka PF, Wong J, Caputo GA, Yin H (2008) Peptide probes for protein transmembrane domains. ACS Chem Biol 3 (7):402-411. doi: 10.1021/cb800049w
    • (2008) ACS Chem Biol , vol.3 , Issue.7 , pp. 402-411
    • Slivka, P.F.1    Wong, J.2    Caputo, G.A.3    Yin, H.4
  • 6
    • 0019891830 scopus 로고
    • Fluorescence quenching in model membranes. Relationship between calcium adenosinetriphosphatase enzyme activity and the affinity of the protein for phosphatidylcholines with different acyl chain characteristics
    • Caffrey M, Feigenson GW (1981) Fluorescence quenching in model membranes. Relationship between calcium adenosinetriphosphatase enzyme activity and the affinity of the protein for phosphatidylcholines with different acyl chain characteristics. Biochemistry 20 (7):1949-1961
    • (1981) Biochemistry , vol.20 , Issue.7 , pp. 1949-1961
    • Caffrey, M.1    Feigenson, G.W.2
  • 7
    • 79958841994 scopus 로고    scopus 로고
    • Light-induced conformational changes in photosynthetic reaction centers: Impact of detergents and lipids on the electronic structure of the primary electron donor
    • doi: 10.1021/bi200595z
    • Deshmukh SS, Akhavein H, Williams JC, Allen JP, Kalman L (2011) Light-induced conformational changes in photosynthetic reaction centers: impact of detergents and lipids on the electronic structure of the primary electron donor. Biochemistry 50 (23): 5249-5262. doi: 10.1021/bi200595z
    • (2011) Biochemistry , vol.50 , Issue.23 , pp. 5249-5262
    • Deshmukh, S.S.1    Akhavein, H.2    Williams, J.C.3    Allen, J.P.4    Kalman, L.5
  • 8
    • 0025876658 scopus 로고
    • Hydrophobic membrane thickness and lipid-protein interactions of the leucine transport system of Lactococcus lactis
    • In't Veld G, Driessen AJ, Op den Kamp JA, Konings WN (1991) Hydrophobic membrane thickness and lipid-protein interactions of the leucine transport system of Lactococcus lactis. Biochim Biophys Acta 1065 (2):203-212
    • (1991) Biochim Biophys Acta , vol.1065 , Issue.2 , pp. 203-212
    • In'T Veld, G.1    Driessen, A.J.2    Op Den Kamp, J.A.3    Konings, W.N.4
  • 9
    • 0020486964 scopus 로고
    • Bilayer thickness and enzymatic activity in the mitochondrial cytochrome c oxidase and ATPase complex
    • Montecucco C, Smith GA, Dabbeni-sala F, Johannsson A, Galante YM, Bisson R (1982) Bilayer thickness and enzymatic activity in the mitochondrial cytochrome c oxidase and ATPase complex. FEBS Lett 144 (1):145-148
    • (1982) FEBS Lett , vol.144 , Issue.1 , pp. 145-148
    • Montecucco, C.1    Smith, G.A.2    Dabbeni-Sala, F.3    Johannsson, A.4    Galante, Y.M.5    Bisson, R.6
  • 10
    • 0035902530 scopus 로고    scopus 로고
    • Effects of bilayer thickness on the activity of diacylglycerol kinase of Escherichia coli
    • Pilot JD, East JM, Lee AG (2001) Effects of bilayer thickness on the activity of diacylglycerol kinase of Escherichia coli. Biochemistry 40 (28):8188-8195
    • (2001) Biochemistry , vol.40 , Issue.28 , pp. 8188-8195
    • Pilot, J.D.1    East, J.M.2    Lee, A.G.3
  • 11
    • 34347262391 scopus 로고    scopus 로고
    • Bilayer thickness and membrane protein function: An energetic perspective
    • doi: 10.1146/ annurev.biophys.36.040306.132643
    • Andersen OS, Koeppe RE II (2007) Bilayer thickness and membrane protein function: an energetic perspective. Annu Rev Biophys Biomol Struct 36:107-130. doi: 10.1146/ annurev.biophys.36.040306.132643
    • (2007) Annu Rev Biophys Biomol Struct , vol.36 , pp. 107-130
    • Andersen, O.S.1    Koeppe, R.E.I.I.2
  • 13
    • 77954299061 scopus 로고    scopus 로고
    • A comprehensive comparison of transmembrane domains reveals organelle-specific properties
    • doi: 10.1016/j.cell. 2010.05.037
    • Sharpe HJ, Stevens TJ, Munro S (2010) A comprehensive comparison of transmembrane domains reveals organelle-specific properties. Cell 142 (1):158-169. doi: 10.1016/j.cell. 2010.05.037
    • (2010) Cell , vol.142 , Issue.1 , pp. 158-169
    • Sharpe, H.J.1    Stevens, T.J.2    Munro, S.3
  • 14
    • 0031740415 scopus 로고    scopus 로고
    • Hydrophobic mismatch between proteins and lipids in membranes
    • Killian JA (1998) Hydrophobic mismatch between proteins and lipids in membranes. Biochim Biophys Acta 1376 (3):401-415
    • (1998) Biochim Biophys Acta , vol.1376 , Issue.3 , pp. 401-415
    • Killian, J.A.1
  • 15
    • 0034284386 scopus 로고    scopus 로고
    • How proteins adapt to a membrane-water interface
    • Killian JA, von Heijne G (2000) How proteins adapt to a membrane-water interface. Trends Biochem Sci 25 (9):429-434
    • (2000) Trends Biochem Sci , vol.25 , Issue.9 , pp. 429-434
    • Killian, J.A.1    Von Heijne, G.2
  • 16
    • 0037465834 scopus 로고    scopus 로고
    • Cumulative effects of amino acid substitutions and hydrophobic mismatch upon the transmembrane stability and conformation of hydrophobic alpha-helices
    • doi: 10.1021/bi026697d
    • Caputo GA, London E (2003) Cumulative effects of amino acid substitutions and hydrophobic mismatch upon the transmembrane stability and conformation of hydrophobic alpha-helices. Biochemistry 42 (11):3275-3285. doi: 10.1021/bi026697d
    • (2003) Biochemistry , vol.42 , Issue.11 , pp. 3275-3285
    • Caputo, G.A.1    London, E.2
  • 17
    • 0027892019 scopus 로고
    • Cholesterol and the Golgi apparatus
    • Bretscher MS, Munro S (1993) Cholesterol and the Golgi apparatus. Science 261 (5126): 1280-1281
    • (1993) Science , vol.261 , Issue.5126 , pp. 1280-1281
    • Bretscher, M.S.1    Munro, S.2
  • 18
    • 0036725152 scopus 로고    scopus 로고
    • Physical principles underlying the transduction of bilayer deformation forces during mechanosensitive channel gating
    • doi: 10.1038/ nsb827
    • Perozo E, Kloda A, Cortes DM, Martinac B (2002) Physical principles underlying the transduction of bilayer deformation forces during mechanosensitive channel gating. Nat Struct Biol 9 (9):696-703. doi: 10.1038/ nsb827
    • (2002) Nat Struct Biol , vol.9 , Issue.9 , pp. 696-703
    • Perozo, E.1    Kloda, A.2    Cortes, D.M.3    Martinac, B.4
  • 20
    • 0032581038 scopus 로고    scopus 로고
    • Influence of lipid/peptide hydrophobic mismatch on the thickness of diacylphosphatidylcholine bilayers. A 2H NMR and ESR study using designed transmembrane alpha-helical peptides and gramicidin A
    • doi: 10.1021/bi980233r
    • de Planque MR, Greathouse DV, Koeppe RE II, Schafer H, Marsh D, Killian JA (1998) Influence of lipid/peptide hydrophobic mismatch on the thickness of diacylphosphatidylcholine bilayers. A 2H NMR and ESR study using designed transmembrane alpha-helical peptides and gramicidin A. Biochemistry 37 (26):9333-9345. doi: 10.1021/bi980233r
    • (1998) Biochemistry , vol.37 , Issue.26 , pp. 9333-9345
    • De Planque, M.R.1    Greathouse, D.V.2    Koeppe, R.E.I.I.3    Schafer, H.4    Marsh, D.5    Killian, J.A.6
  • 21
    • 77956579453 scopus 로고    scopus 로고
    • Influence of hydrophobic mismatch and amino acid composition on the lateral diffusion of transmembrane peptides
    • doi: 10.1016/j. bpj.2010.05.042
    • Ramadurai S, Holt A, Schafer LV, Krasnikov VV, Rijkers DT, Marrink SJ, Killian JA, Poolman B (2010) Influence of hydrophobic mismatch and amino acid composition on the lateral diffusion of transmembrane peptides. Biophys J 99 (5):1447-1454. doi: 10.1016/j. bpj.2010.05.042
    • (2010) Biophys J , vol.99 , Issue.5 , pp. 1447-1454
    • Ramadurai, S.1    Holt, A.2    Schafer, L.V.3    Krasnikov, V.V.4    Rijkers, D.T.5    Marrink, S.J.6    Killian, J.A.7    Poolman, B.8
  • 22
    • 0034696524 scopus 로고    scopus 로고
    • Tryptophan-anchored transmembrane peptides promote formation of nonlamellar phases in phosphatidylethanolamine model membranes in a mismatch-dependent manner
    • van der Wel PC, Pott T, Morein S, Greathouse DV, Koeppe RE II, Killian JA (2000) Tryptophan-anchored transmembrane peptides promote formation of nonlamellar phases in phosphatidylethanolamine model membranes in a mismatch-dependent manner. Biochemistry 39 (11):3124-3133
    • (2000) Biochemistry , vol.39 , Issue.11 , pp. 3124-3133
    • Van Der Wel, P.C.1    Pott, T.2    Morein, S.3    Greathouse, D.V.4    Koeppe, R.E.I.I.5    Killian, J.A.6
  • 23
    • 0026442901 scopus 로고
    • Interaction of a peptide model of a hydrophobic transmembrane alpha-helical segment of a membrane protein with phosphatidylcholine bilayers: Differential scanning calorimetric and FTIR spectroscopic studies
    • Zhang YP, Lewis RN, Hodges RS, McElhaney RN (1992) Interaction of a peptide model of a hydrophobic transmembrane alpha-helical segment of a membrane protein with phosphatidylcholine bilayers: differential scanning calorimetric and FTIR spectroscopic studies. Biochemistry 31 (46):11579-11588
    • (1992) Biochemistry , vol.31 , Issue.46 , pp. 11579-11588
    • Zhang, Y.P.1    Lewis, R.N.2    Hodges, R.S.3    McElhaney, R.N.4
  • 24
    • 35548971929 scopus 로고    scopus 로고
    • Effect of sequence hydrophobicity and bilayer width upon the minimum length required for the formation of transmembrane helices in membranes
    • Krishnakumar SS, London E (2007) Effect of sequence hydrophobicity and bilayer width upon the minimum length required for the formation of transmembrane helices in membranes. J Mol Biol 374 (3):671-687
    • (2007) J Mol Biol , vol.374 , Issue.3 , pp. 671-687
    • Krishnakumar, S.S.1    London, E.2
  • 25
    • 77954371031 scopus 로고    scopus 로고
    • Revisiting hydrophobic mismatch with free energy simulation studies of transmembrane helix tilt and rotation
    • doi: 10.1016/j. bpj.2010.04.015
    • Kim T, Im W (2010) Revisiting hydrophobic mismatch with free energy simulation studies of transmembrane helix tilt and rotation. Biophys J 99 (1):175-183. doi: 10.1016/j. bpj.2010.04.015
    • (2010) Biophys J , vol.99 , Issue.1 , pp. 175-183
    • Kim, T.1    Im, W.2
  • 26
    • 0032512417 scopus 로고    scopus 로고
    • Hydrophobic mismatch and the incorporation of peptides into lipid bilayers: A possible mechanism for retention in the Golgi
    • doi: 10.1021/bi972441+
    • Webb RJ, East JM, Sharma RP, Lee AG (1998) Hydrophobic mismatch and the incorporation of peptides into lipid bilayers: a possible mechanism for retention in the Golgi. Biochemistry 37 (2):673-679. doi: 10.1021/bi972441+
    • (1998) Biochemistry , vol.37 , Issue.2 , pp. 673-679
    • Webb, R.J.1    East, J.M.2    Sharma, R.P.3    Lee, A.G.4
  • 27
    • 12244255728 scopus 로고    scopus 로고
    • Hydrophobic mismatch between helices and lipid bilayers
    • doi: 10.1016/ S0006-3495(03)74858-9
    • Weiss TM, van der Wel PC, Killian JA, Koeppe RE II, Huang HW (2003) Hydrophobic mismatch between helices and lipid bilayers. Biophys J 84 (1):379-385. doi: 10.1016/ S0006-3495 (03)74858-9
    • (2003) Biophys J , vol.84 , Issue.1 , pp. 379-385
    • Weiss, T.M.1    Van Der Wel, P.C.2    Killian, J.A.3    Koeppe, R.E.I.I.4    Huang, H.W.5
  • 28
    • 0036199831 scopus 로고    scopus 로고
    • Characterization of the thermotropic behavior and lateral organization of lipid-peptide mixtures by a combined experimental and theoretical approach: Effects of hydrophobic mismatch and role of flanking residues
    • doi: 10.1016/ S0006-3495 (02)75495-7
    • Morein S, Killian JA, Sperotto MM (2002) Characterization of the thermotropic behavior and lateral organization of lipid-peptide mixtures by a combined experimental and theoretical approach: effects of hydrophobic mismatch and role of flanking residues. Biophys J 82 (3):1405-1417. doi: 10.1016/ S0006-3495 (02)75495-7
    • (2002) Biophys J , vol.82 , Issue.3 , pp. 1405-1417
    • Morein, S.1    Killian, J.A.2    Sperotto, M.M.3
  • 29
    • 0034108440 scopus 로고    scopus 로고
    • The effect of peptide/ lipid hydrophobic mismatch on the phase behavior of model membranes mimicking the lipid composition in Escherichia coli membranes
    • Morein S, Koeppe IR, Lindblom G, de Kruijff B, Killian JA (2000) The effect of peptide/ lipid hydrophobic mismatch on the phase behavior of model membranes mimicking the lipid composition in Escherichia coli membranes. Biophys J 78 (5):2475-2485
    • (2000) Biophys J , vol.78 , Issue.5 , pp. 2475-2485
    • Morein, S.1    Koeppe, I.R.2    Lindblom, G.3    De Kruijff, B.4    Killian, J.A.5
  • 30
    • 33646198955 scopus 로고    scopus 로고
    • Molecular dynamics simulations of model transmembrane peptides in lipid bilayers: A systematic investigation of hydrophobic mismatch
    • doi: 10.1529/ biophysj.105.073395
    • Kandasamy SK, Larson RG (2006) Molecular dynamics simulations of model transmembrane peptides in lipid bilayers: a systematic investigation of hydrophobic mismatch. Biophys J 90 (7):2326-2343. doi: 10.1529/ biophysj.105.073395
    • (2006) Biophys J , vol.90 , Issue.7 , pp. 2326-2343
    • Kandasamy, S.K.1    Larson, R.G.2
  • 31
    • 77952257688 scopus 로고    scopus 로고
    • Order parameters of a transmembrane helix in a fluid bilayer: Case study of a WALP peptide
    • doi: 10.1016/j. bpj.2010.01.016
    • Holt A, Rougier L, Reat V, Jolibois F, Saurel O, Czaplicki J, Killian JA, Milon A (2010) Order parameters of a transmembrane helix in a fluid bilayer: case study of a WALP peptide. Biophys J 98 (9):1864-1872. doi: 10.1016/j. bpj.2010.01.016
    • (2010) Biophys J , vol.98 , Issue.9 , pp. 1864-1872
    • Holt, A.1    Rougier, L.2    Reat, V.3    Jolibois, F.4    Saurel, O.5    Czaplicki, J.6    Killian, J.A.7    Milon, A.8
  • 32
    • 0037062590 scopus 로고    scopus 로고
    • Lipid dependence of membrane anchoring properties and snorkeling behavior of aromatic and charged residues in transmembrane peptides
    • Strandberg E, Morein S, Rijkers DT, Liskamp RM, van der Wel PC, Killian JA (2002) Lipid dependence of membrane anchoring properties and snorkeling behavior of aromatic and charged residues in transmembrane peptides. Biochemistry 41 (23):7190-7198
    • (2002) Biochemistry , vol.41 , Issue.23 , pp. 7190-7198
    • Strandberg, E.1    Morein, S.2    Rijkers, D.T.3    Liskamp, R.M.4    Van Der Wel, P.C.5    Killian, J.A.6
  • 33
    • 0037162409 scopus 로고    scopus 로고
    • Effect of variations in the structure of a polyleucine-based alpha-helical transmembrane peptide on its interaction with phosphatidylcholine bilayers
    • Liu F, Lewis RN, Hodges RS, McElhaney RN (2002) Effect of variations in the structure of a polyleucine-based alpha-helical transmembrane peptide on its interaction with phosphatidylcholine bilayers. Biochemistry 41 (29):9197-9207
    • (2002) Biochemistry , vol.41 , Issue.29 , pp. 9197-9207
    • Liu, F.1    Lewis, R.N.2    Hodges, R.S.3    McElhaney, R.N.4
  • 34
    • 16644377766 scopus 로고    scopus 로고
    • Effect of variations in the structure of a polyleucine-based alpha-helical transmembrane peptide on its interaction with phosphatidylethanolamine Bilayers
    • doi: 10.1529/biophysj.104.046342
    • Liu F, Lewis RN, Hodges RS, McElhaney RN (2004) Effect of variations in the structure of a polyleucine-based alpha-helical transmembrane peptide on its interaction with phosphatidylethanolamine Bilayers. Biophys J 87 (4):2470-2482. doi: 10.1529/biophysj.104.046342
    • (2004) Biophys J , vol.87 , Issue.4 , pp. 2470-2482
    • Liu, F.1    Lewis, R.N.2    Hodges, R.S.3    McElhaney, R.N.4
  • 35
    • 1642279990 scopus 로고    scopus 로고
    • Effect of variations in the structure of a polyleucine-based alpha-helical transmembrane peptide on its interaction with phosphatidylglycerol bilayers
    • doi: 10.1021/bi036214l
    • Liu F, Lewis RN, Hodges RS, McElhaney RN (2004) Effect of variations in the structure of a polyleucine-based alpha-helical transmembrane peptide on its interaction with phosphatidylglycerol bilayers. Biochemistry 43 (12): 3679-3687. doi: 10.1021/bi036214l
    • (2004) Biochemistry , vol.43 , Issue.12 , pp. 3679-3687
    • Liu, F.1    Lewis, R.N.2    Hodges, R.S.3    McElhaney, R.N.4
  • 36
    • 0028941129 scopus 로고
    • Interaction of a peptide model of a hydrophobic transmembrane alpha-helical segment of a membrane protein with phosphatidylethanolamine bilayers: Differential scanning calorimetric and Fourier transform infrared spectroscopic studies
    • doi: 10.1016/S0006-3495 (95)80261-4
    • Zhang YP, Lewis RN, Hodges RS, McElhaney RN (1995) Interaction of a peptide model of a hydrophobic transmembrane alpha-helical segment of a membrane protein with phosphatidylethanolamine bilayers: differential scanning calorimetric and Fourier transform infrared spectroscopic studies. Biophys J 68 (3):847-857. doi: 10.1016/S0006-3495 (95)80261-4
    • (1995) Biophys J , vol.68 , Issue.3 , pp. 847-857
    • Zhang, Y.P.1    Lewis, R.N.2    Hodges, R.S.3    McElhaney, R.N.4
  • 37
    • 0035895347 scopus 로고    scopus 로고
    • Peptide models of the helical hydrophobic transmembrane segments of membrane proteins: Interactions of acetyl- K2- (LA)12-K2-amide with phosphatidylethanolamine bilayer membranes
    • Zhang YP, Lewis RN, Hodges RS, McElhaney RN (2001) Peptide models of the helical hydrophobic transmembrane segments of membrane proteins: interactions of acetyl- K2- (LA)12-K2-amide with phosphatidylethanolamine bilayer membranes. Biochemistry 40 (2):474-482
    • (2001) Biochemistry , vol.40 , Issue.2 , pp. 474-482
    • Zhang, Y.P.1    Lewis, R.N.2    Hodges, R.S.3    McElhaney, R.N.4
  • 38
    • 3042774119 scopus 로고    scopus 로고
    • Position and ionization state of Asp in the core of membrane- inserted alpha helices control both the equilibrium between transmembrane and nontransmembrane helix topography and transmembrane helix positioning
    • Caputo GA, London E (2004) Position and ionization state of Asp in the core of membrane- inserted alpha helices control both the equilibrium between transmembrane and nontransmembrane helix topography and transmembrane helix positioning. Biochemistry 43 (27):8794-8806
    • (2004) Biochemistry , vol.43 , Issue.27 , pp. 8794-8806
    • Caputo, G.A.1    London, E.2
  • 39
    • 0033522486 scopus 로고    scopus 로고
    • Control of the transmembrane orientation and interhelical interactions within membranes by hydrophobic helix length
    • Ren J, Lew S, Wang J, London E (1999) Control of the transmembrane orientation and interhelical interactions within membranes by hydrophobic helix length. Biochemistry 38 (18):5905-5912
    • (1999) Biochemistry , vol.38 , Issue.18 , pp. 5905-5912
    • Ren, J.1    Lew, S.2    Wang, J.3    London, E.4
  • 40
    • 0030738720 scopus 로고    scopus 로고
    • Transmembrane orientation of hydrophobic alpha-helices is regulated both by the relationship of helix length to bilayer thickness and by the cholesterol concentration
    • Ren J, Lew S, Wang Z, London E (1997) Transmembrane orientation of hydrophobic alpha-helices is regulated both by the relationship of helix length to bilayer thickness and by the cholesterol concentration. Biochemistry 36 (33):10213-10220
    • (1997) Biochemistry , vol.36 , Issue.33 , pp. 10213-10220
    • Ren, J.1    Lew, S.2    Wang, Z.3    London, E.4
  • 41
    • 36248978178 scopus 로고    scopus 로고
    • The control of transmembrane helix transverse position in membranes by hydrophilic residues
    • doi: 10.1016/j.jmb.2007.10.032
    • Krishnakumar SS, London E (2007) The control of transmembrane helix transverse position in membranes by hydrophilic residues. J Mol Biol 374 (5):1251-1269. doi: 10.1016/j.jmb.2007.10.032
    • (2007) J Mol Biol , vol.374 , Issue.5 , pp. 1251-1269
    • Krishnakumar, S.S.1    London, E.2
  • 42
    • 0025269179 scopus 로고
    • Relationships between lipid membrane area, hydrophobic thickness, and acyl-chain orientational order. The effects of cholesterol
    • doi: 10.1016/ S0006-3495(90)82557-82561
    • Ipsen JH, Mouritsen OG, Bloom M (1990) Relationships between lipid membrane area, hydrophobic thickness, and acyl-chain orientational order. The effects of cholesterol. Biophys J 57 (3):405-412. doi: 10.1016/ S0006-3495 (90)82557-1
    • (1990) Biophys J , vol.57 , Issue.3 , pp. 405-412
    • Ipsen, J.H.1    Mouritsen, O.G.2    Bloom, M.3
  • 43
    • 0022718663 scopus 로고
    • Determining bilayer hydrocarbon thickness from neutron diffraction measurements using strip-function models
    • doi: 10.1016/S0006-3495(86)83733-X
    • King GI, White SH (1986) Determining bilayer hydrocarbon thickness from neutron diffraction measurements using strip-function models. Biophys J 49 (5):1047-1054. doi: 10.1016/S0006-3495 (86)83733-X
    • (1986) Biophys J , vol.49 , Issue.5 , pp. 1047-1054
    • King, G.I.1    White, S.H.2
  • 44
    • 0021104058 scopus 로고
    • Lipid bilayer thickness varies linearly with acyl chain length in fluid phosphatidylcholine vesicles
    • Lewis BA, Engelman DM (1983) Lipid bilayer thickness varies linearly with acyl chain length in fluid phosphatidylcholine vesicles. J Mol Biol 166 (2):211-217
    • (1983) J Mol Biol , vol.166 , Issue.2 , pp. 211-217
    • Lewis, B.A.1    Engelman, D.M.2
  • 45
    • 0033932837 scopus 로고    scopus 로고
    • Effect of chain length and unsaturation on elasticity of lipid bilayers
    • doi: 10.1016/S0006-3495 (00)76295-3
    • Rawicz W, Olbrich KC, McIntosh T, Needham D, Evans E (2000) Effect of chain length and unsaturation on elasticity of lipid bilayers. Biophys J 79 (1):328-339. doi: 10.1016/S0006-3495 (00)76295-3
    • (2000) Biophys J , vol.79 , Issue.1 , pp. 328-339
    • Rawicz, W.1    Olbrich, K.C.2    McIntosh, T.3    Needham, D.4    Evans, E.5
  • 46
    • 0037465698 scopus 로고    scopus 로고
    • Using a novel dual fluorescence quenching assay for measurement of tryptophan depth within lipid bilayers to determine hydrophobic alphahelix locations within membranes
    • Caputo GA, London E (2003) Using a novel dual fluorescence quenching assay for measurement of tryptophan depth within lipid bilayers to determine hydrophobic alphahelix locations within membranes. Biochemistry 42 (11):3265-3274
    • (2003) Biochemistry , vol.42 , Issue.11 , pp. 3265-3274
    • Caputo, G.A.1    London, E.2
  • 47
    • 77249173166 scopus 로고    scopus 로고
    • Repositioning of transmembrane alphahelices during membrane protein folding
    • doi: 10.1016/j. jmb.2010.01.042
    • Kauko A, Hedin LE, Thebaud E, Cristobal S, Elofsson A, von Heijne G (2010) Repositioning of transmembrane alphahelices during membrane protein folding. J Mol Biol 397 (1):190-201. doi: 10.1016/j. jmb.2010.01.042
    • (2010) J Mol Biol , vol.397 , Issue.1 , pp. 190-201
    • Kauko, A.1    Hedin, L.E.2    Thebaud, E.3    Cristobal, S.4    Elofsson, A.5    Von Heijne, G.6
  • 48
    • 0037298237 scopus 로고    scopus 로고
    • Stop-transfer efficiency of marginally hydrophobic segments depends on the length of the carboxy-terminal tail
    • doi: 10.1038/sj.embor.embor728
    • Hessa T, Monne M, von Heijne G (2003) Stop-transfer efficiency of marginally hydrophobic segments depends on the length of the carboxy-terminal tail. EMBO Rep 4 (2):178-183 doi: 10.1038/sj.embor.embor728
    • (2003) EMBO Rep , vol.4 , Issue.2 , pp. 178-183
    • Hessa, T.1    Monne, M.2    Von Heijne, G.3
  • 49
    • 0033527670 scopus 로고    scopus 로고
    • Turns in transmembrane helices: Determination of the minimal length of a "helical hairpin" and derivation of a fine- grained turn propensity scale
    • doi: 10.1006/jmbi.1999.3183
    • Monne M, Nilsson I, Elofsson A, von Heijne G (1999) Turns in transmembrane helices: determination of the minimal length of a "helical hairpin" and derivation of a fine- grained turn propensity scale. J Mol Biol 293 (4):807-814. doi: 10.1006/jmbi.1999.3183
    • (1999) J Mol Biol , vol.293 , Issue.4 , pp. 807-814
    • Monne, M.1    Nilsson, I.2    Elofsson, A.3    Von Heijne, G.4
  • 50
    • 0032509124 scopus 로고    scopus 로고
    • Positively and negatively charged residues have different effects on the position in the membrane of a model transmembrane helix
    • doi: 10.1006/jmbi.1998.2218
    • Monne M, Nilsson I, Johansson M, Elmhed N, von Heijne G (1998) Positively and negatively charged residues have different effects on the position in the membrane of a model transmembrane helix. J Mol Biol 284 (4):1177-1183. doi: 10.1006/jmbi.1998.2218
    • (1998) J Mol Biol , vol.284 , Issue.4 , pp. 1177-1183
    • Monne, M.1    Nilsson, I.2    Johansson, M.3    Elmhed, N.4    Von Heijne, G.5
  • 51
    • 0032509102 scopus 로고    scopus 로고
    • Prolineinduced disruption of a transmembrane alpha-helix in its natural environment
    • doi: 10.1006/ jmbi.1998.2217
    • Nilsson I, Saaf A, Whitley P, Gafvelin G, Waller C, von Heijne G (1998) Prolineinduced disruption of a transmembrane alpha-helix in its natural environment. J Mol Biol 284 (4):1165-1175. doi: 10.1006/ jmbi.1998.2217
    • (1998) J Mol Biol , vol.284 , Issue.4 , pp. 1165-1175
    • Nilsson, I.1    Saaf, A.2    Whitley, P.3    Gafvelin, G.4    Waller, C.5    Von Heijne, G.6
  • 52
    • 0026071516 scopus 로고
    • Monte Carlo simulation studies of lipid order parameter profiles near integral membrane proteins
    • doi: 10.1016/ S0006-3495 (91)82219-6
    • Sperotto MM, Mouritsen OG (1991) Monte Carlo simulation studies of lipid order parameter profiles near integral membrane proteins. Biophys J 59 (2):261-270. doi: 10.1016/ S0006-3495 (91)82219-6
    • (1991) Biophys J , vol.59 , Issue.2 , pp. 261-270
    • Sperotto, M.M.1    Mouritsen, O.G.2
  • 53
    • 0033038093 scopus 로고    scopus 로고
    • Theoretical analysis of hydrophobic matching and membranemediated interactions in lipid bilayers containing gramicidin
    • doi: 10.1016/S0006-3495 (99)77469-2
    • Harroun TA, Heller WT, Weiss TM, Yang L, Huang HW (1999) Theoretical analysis of hydrophobic matching and membranemediated interactions in lipid bilayers containing gramicidin. Biophys J 76 (6):3176-3185. doi: 10.1016/S0006-3495 (99)77469-2
    • (1999) Biophys J , vol.76 , Issue.6 , pp. 3176-3185
    • Harroun, T.A.1    Heller, W.T.2    Weiss, T.M.3    Yang, L.4    Huang, H.W.5
  • 54
    • 0032988823 scopus 로고    scopus 로고
    • Experimental evidence for hydrophobic matching and membranemediated interactions in lipid bilayers containing gramicidin
    • doi: 10.1016/S0006-3495 (99)77257-7
    • Harroun TA, Heller WT, Weiss TM, Yang L, Huang HW (1999) Experimental evidence for hydrophobic matching and membranemediated interactions in lipid bilayers containing gramicidin. Biophys J 76 (2):937-945. doi: 10.1016/S0006-3495 (99)77257-7
    • (1999) Biophys J , vol.76 , Issue.2 , pp. 937-945
    • Harroun, T.A.1    Heller, W.T.2    Weiss, T.M.3    Yang, L.4    Huang, H.W.5
  • 55
    • 0035936573 scopus 로고    scopus 로고
    • A differential scanning calorimetric and 31P NMR spectroscopic study of the effect of transmembrane alpha-helical peptides on the lamellar-reversed hexagonal phase transition of phosphatidylethanolamine model membranes
    • Liu F, Lewis RN, Hodges RS, McElhaney RN (2001) A differential scanning calorimetric and 31P NMR spectroscopic study of the effect of transmembrane alpha-helical peptides on the lamellar-reversed hexagonal phase transition of phosphatidylethanolamine model membranes. Biochemistry 40 (3):760-768
    • (2001) Biochemistry , vol.40 , Issue.3 , pp. 760-768
    • Liu, F.1    Lewis, R.N.2    Hodges, R.S.3    McElhaney, R.N.4
  • 56
    • 0033783447 scopus 로고    scopus 로고
    • Alignment of lysine-anchored membrane peptides under conditions of hydrophobic mismatch: A CD, 15N and 31P solid-state NMR spectroscopy investigation
    • Harzer U, Bechinger B (2000) Alignment of lysine-anchored membrane peptides under conditions of hydrophobic mismatch: a CD, 15N and 31P solid-state NMR spectroscopy investigation. Biochemistry 39 (43):13106-13114
    • (2000) Biochemistry , vol.39 , Issue.43 , pp. 13106-13114
    • Harzer, U.1    Bechinger, B.2
  • 57
    • 15244348542 scopus 로고    scopus 로고
    • The conformation of the pore region of the M2 proton channel depends on lipid bilayer environment
    • doi: 10.1110/ps.041185805
    • Duong-Ly KC, Nanda V, Degrado WF, Howard KP (2005) The conformation of the pore region of the M2 proton channel depends on lipid bilayer environment. Protein Sci 14 (4):856-861. doi: 10.1110/ps.041185805
    • (2005) Protein Sci , vol.14 , Issue.4 , pp. 856-861
    • Duong-Ly, K.C.1    Nanda, V.2    Degrado, W.F.3    Howard, K.P.4
  • 59
    • 2942662220 scopus 로고    scopus 로고
    • Tilt angles of transmembrane model peptides in oriented and nonoriented lipid bilayers as determined by 2H solid-state NMR
    • doi: 10.1529/biophysj.103.035402
    • Strandberg E, Ozdirekcan S, Rijkers DT, van der Wel PC, Koeppe RE II, Liskamp RM, Killian JA (2004) Tilt angles of transmembrane model peptides in oriented and nonoriented lipid bilayers as determined by 2H solid-state NMR. Biophys J 86 (6):3709-3721. doi: 10.1529/biophysj.103.035402
    • (2004) Biophys J , vol.86 , Issue.6 , pp. 3709-3721
    • Strandberg, E.1    Ozdirekcan, S.2    Rijkers, D.T.3    Van Der Wel, P.C.4    Koeppe, R.E.I.I.5    Liskamp, R.M.6    Killian, J.A.7
  • 60
    • 0036708458 scopus 로고    scopus 로고
    • Geometry and intrinsic tilt of a tryptophan-anchored transmembrane alpha-helix determined by (2)H NMR
    • doi: 10.1016/ S0006-3495 (02)73918-0
    • van der Wel PC, Strandberg E, Killian JA, Koeppe RE II (2002) Geometry and intrinsic tilt of a tryptophan-anchored transmembrane alpha-helix determined by (2)H NMR. Biophys J 83 (3):1479-1488. doi: 10.1016/ S0006-3495 (02)73918-0
    • (2002) Biophys J , vol.83 , Issue.3 , pp. 1479-1488
    • Van Der Wel, P.C.1    Strandberg, E.2    Killian, J.A.3    Koeppe, R.E.I.I.4
  • 61
    • 0035942298 scopus 로고    scopus 로고
    • Sensitivity of single membrane-spanning alpha-helical peptides to hydrophobic mismatch with a lipid bilayer: Effects on backbone structure, orientation, and extent of membrane incorporation
    • de Planque MR, Goormaghtigh E, Greathouse DV, Koeppe RE II, Kruijtzer JA, Liskamp RM, de Kruijff B, Killian JA (2001) Sensitivity of single membrane-spanning alpha-helical peptides to hydrophobic mismatch with a lipid bilayer: effects on backbone structure, orientation, and extent of membrane incorporation. Biochemistry 40 (16):5000-5010
    • (2001) Biochemistry , vol.40 , Issue.16 , pp. 5000-5010
    • De Planque, M.R.1    Goormaghtigh, E.2    Greathouse, D.V.3    Koeppe, R.E.I.I.4    Kruijtzer, J.A.5    Liskamp, R.M.6    De Kruijff, B.7    Killian, J.A.8
  • 62
    • 56049103780 scopus 로고    scopus 로고
    • Conformation and membrane orientation of amphiphilic helical peptides by oriented circular dichroism
    • doi: 10.1529/biophysj.108.136085
    • Burck J, Roth S, Wadhwani P, Afonin S, Kanithasen N, Strandberg E, Ulrich AS (2008) Conformation and membrane orientation of amphiphilic helical peptides by oriented circular dichroism. Biophys J 95 (8):3872-3881. doi: 10.1529/biophysj.108.136085
    • (2008) Biophys J , vol.95 , Issue.8 , pp. 3872-3881
    • Burck, J.1    Roth, S.2    Wadhwani, P.3    Afonin, S.4    Kanithasen, N.5    Strandberg, E.6    Ulrich, A.S.7
  • 63
    • 0034738609 scopus 로고    scopus 로고
    • Oriented circular dichroism of a class A amphipathic helix in aligned phospholipid multilayers
    • Clayton AH, Sawyer WH (2000) Oriented circular dichroism of a class A amphipathic helix in aligned phospholipid multilayers. Biochim Biophys Acta 1467 (1):124-130
    • (2000) Biochim Biophys Acta , vol.1467 , Issue.1 , pp. 124-130
    • Clayton, A.H.1    Sawyer, W.H.2
  • 64
    • 0342804291 scopus 로고    scopus 로고
    • Chirality and circular dichroism of oriented molecules and anisotropic phases
    • Kuball HG, Hofer T (2000) Chirality and circular dichroism of oriented molecules and anisotropic phases. Chirality 12 (4):278-286. doi: 10.1002/ (SICI)1520-636X (2000)12: 43.0.CO;2-O
    • (2000) Chirality , vol.12 , Issue.4 , pp. 278-286
    • Kuball, H.G.1    Hofer, T.2
  • 65
    • 0028598299 scopus 로고
    • Analysis of circular dichroism spectra of oriented protein-lipid complexes: Toward a general application
    • de Jongh HH, Goormaghtigh E, Killian JA (1994) Analysis of circular dichroism spectra of oriented protein-lipid complexes: toward a general application. Biochemistry 33 (48): 14521-14528
    • (1994) Biochemistry , vol.33 , Issue.48 , pp. 14521-14528
    • De Jongh, H.H.1    Goormaghtigh, E.2    Killian, J.A.3
  • 66
    • 0025278431 scopus 로고
    • Method of oriented circular dichroism
    • doi: 10.1016/S0006-3495 (90)82599-6
    • Wu Y, Huang HW, Olah GA (1990) Method of oriented circular dichroism. Biophys J 57 (4):797-806. doi: 10.1016/S0006-3495 (90)82599-6
    • (1990) Biophys J , vol.57 , Issue.4 , pp. 797-806
    • Wu, Y.1    Huang, H.W.2    Olah, G.A.3
  • 67
    • 0034459184 scopus 로고    scopus 로고
    • Attenuated total reflection IR spectroscopy as a tool to investigate the structure, orientation and tertiary structure changes in peptides and membrane proteins
    • Vigano C, Manciu L, Buyse F, Goormaghtigh E, Ruysschaert JM (2000) Attenuated total reflection IR spectroscopy as a tool to investigate the structure, orientation and tertiary structure changes in peptides and membrane proteins. Biopolymers 55 (5):373-380. d o i : 10.1002/1097- 0282 (2000)55: 53.0.CO;2-U
    • (2000) Biopolymers , vol.55 , Issue.5 , pp. 373-380
    • Vigano, C.1    Manciu, L.2    Buyse, F.3    Goormaghtigh, E.4    Ruysschaert, J.M.5
  • 68
    • 0027367861 scopus 로고
    • Interaction of myelin basic protein with single bilayers on a solid support: An NMR, DSC and polarized infrared ATR study
    • Reinl HM, Bayerl TM (1993) Interaction of myelin basic protein with single bilayers on a solid support: an NMR, DSC and polarized infrared ATR study. Biochim Biophys Acta 1151 (2):127-136
    • (1993) Biochim Biophys Acta , vol.1151 , Issue.2 , pp. 127-136
    • Reinl, H.M.1    Bayerl, T.M.2
  • 69
    • 0025993413 scopus 로고
    • Orientation of melittin in phospholipid bilayers. A polarized attenuated total reflection infrared study
    • doi: 10.1016/ S0006-3495 (91)82126-9
    • Frey S, Tamm LK (1991) Orientation of melittin in phospholipid bilayers. A polarized attenuated total reflection infrared study. Biophys J 60 (4):922-930. doi: 10.1016/ S0006-3495 (91)82126-9
    • (1991) Biophys J , vol.60 , Issue.4 , pp. 922-930
    • Frey, S.1    Tamm, L.K.2
  • 72
    • 0028879250 scopus 로고
    • The infrared dichroism of transmembrane helical polypeptides
    • doi: 10.1016/ S0006-3495 (95)80150-5
    • Axelsen PH, Kaufman BK, McElhaney RN, Lewis RN (1995) The infrared dichroism of transmembrane helical polypeptides. Biophys J 69 (6):2770-2781. doi: 10.1016/ S0006-3495 (95)80150-5
    • (1995) Biophys J , vol.69 , Issue.6 , pp. 2770-2781
    • Axelsen, P.H.1    Kaufman, B.K.2    McElhaney, R.N.3    Lewis, R.N.4
  • 73
    • 78650627501 scopus 로고    scopus 로고
    • Membrane docking of the C2 domain from protein kinase Calpha as seen by polarized ATR-IR. The role of PIP (2)
    • doi: 10.1016/j.bbamem.2010.11.035
    • Ausili A, Corbalan-Garcia S, Gomez- Fernandez JC, Marsh D (2011) Membrane docking of the C2 domain from protein kinase Calpha as seen by polarized ATR-IR. The role of PIP (2). Biochim Biophys Acta 1808 (3):684-695. doi: 10.1016/j.bbamem.2010.11.035
    • (2011) Biochim Biophys Acta , vol.1808 , Issue.3 , pp. 684-695
    • Ausili, A.1    Corbalan-Garcia, S.2    Gomez-Fernandez, J.C.3    Marsh, D.4
  • 74
    • 70350322975 scopus 로고    scopus 로고
    • In-plane and out-of-plane infrared difference spectroscopy unravels tilting of helices and structural changes in a membrane protein upon substrate binding
    • doi: 10.1021/ ja906324z
    • Lorenz-Fonfria VA, Granell M, Leon X, Leblanc G, Padros E (2009) In-plane and out-of-plane infrared difference spectroscopy unravels tilting of helices and structural changes in a membrane protein upon substrate binding. J Am Chem Soc 131 (42):15094-15095. doi: 10.1021/ ja906324z
    • (2009) J Am Chem Soc , vol.131 , Issue.42 , pp. 15094-15095
    • Lorenz-Fonfria, V.A.1    Granell, M.2    Leon, X.3    Leblanc, G.4    Padros, E.5
  • 75
    • 0037379072 scopus 로고    scopus 로고
    • How do helix-helix interactions help determine the folds of membrane proteins? Perspectives from the study of homooligomeric helical bundles
    • DeGrado WF, Gratkowski H, Lear JD (2003) How do helix-helix interactions help determine the folds of membrane proteins? Perspectives from the study of homooligomeric helical bundles. Protein Sci 12 (4): 647-665
    • (2003) Protein Sci , vol.12 , Issue.4 , pp. 647-665
    • Degrado, W.F.1    Gratkowski, H.2    Lear, J.D.3
  • 76
    • 13844284976 scopus 로고    scopus 로고
    • Association of a model transmembrane peptide containing gly in a heptad sequence motif
    • doi: 10.1529/biophysj.103.032839
    • Lear JD, Stouffer AL, Gratkowski H, Nanda V, Degrado WF (2004) Association of a model transmembrane peptide containing gly in a heptad sequence motif. Biophys J 87 (5):3421-3429. doi: 10.1529/biophysj.103.032839
    • (2004) Biophys J , vol.87 , Issue.5 , pp. 3421-3429
    • Lear, J.D.1    Stouffer, A.L.2    Gratkowski, H.3    Nanda, V.4    Degrado, W.F.5
  • 77
    • 0029117442 scopus 로고
    • Theory and application of fluorescence homotransfer to melittin oligomerization
    • doi: 10.1016/S0006-3495 (95)80030-5
    • Runnels LW, Scarlata SF (1995) Theory and application of fluorescence homotransfer to melittin oligomerization. Biophys J 69 (4): 1569-1583. doi: 10.1016/S0006-3495 (95) 80030-5
    • (1995) Biophys J , vol.69 , Issue.4 , pp. 1569-1583
    • Runnels, L.W.1    Scarlata, S.F.2
  • 78
    • 15544385324 scopus 로고    scopus 로고
    • Forster resonance energy transfer in liposomes: Measurements of transmembrane helix dimerization in the native bilayer environment
    • doi: 10.1016/j.ab.2005.01.035
    • You M, Li E, Wimley WC, Hristova K (2005) Forster resonance energy transfer in liposomes: measurements of transmembrane helix dimerization in the native bilayer environment. Anal Biochem 340 (1):154-164. doi: 10.1016/j.ab.2005.01.035
    • (2005) Anal Biochem , vol.340 , Issue.1 , pp. 154-164
    • You, M.1    Li, E.2    Wimley, W.C.3    Hristova, K.4
  • 79
    • 0041317291 scopus 로고    scopus 로고
    • The effect of interactions involving ionizable residues flanking membrane-inserted hydrophobic helices upon helix-helix interaction
    • Lew S, Caputo GA, London E (2003) The effect of interactions involving ionizable residues flanking membrane-inserted hydrophobic helices upon helix-helix interaction. Biochemistry 42 (36):10833-10842
    • (2003) Biochemistry , vol.42 , Issue.36 , pp. 10833-10842
    • Lew, S.1    Caputo, G.A.2    London, E.3
  • 80
    • 0031571617 scopus 로고    scopus 로고
    • Simple procedure for reversed-phase high-performance liquid chromatographic purification of long hydrophobic peptides that form transmembrane helices
    • Lew S, London E (1997) Simple procedure for reversed-phase high-performance liquid chromatographic purification of long hydrophobic peptides that form transmembrane helices. Anal Biochem 251 (1):113-116
    • (1997) Anal Biochem , vol.251 , Issue.1 , pp. 113-116
    • Lew, S.1    London, E.2
  • 81
    • 0031005647 scopus 로고    scopus 로고
    • Distribution analysis of depth-dependent fluorescence quenching in membranes: A practical guide
    • Ladokhin AS (1997) Distribution analysis of depth-dependent fluorescence quenching in membranes: a practical guide. Methods Enzymol 278:462-473
    • (1997) Methods Enzymol , vol.278 , pp. 462-473
    • Ladokhin, A.S.1
  • 82
    • 0026766835 scopus 로고
    • Calibration of the parallax fluorescence quenching method for determination of membrane penetration depth: Refinement and comparison of quenching by spin-labeled and brominated lipids
    • Abrams FS, London E (1992) Calibration of the parallax fluorescence quenching method for determination of membrane penetration depth: refinement and comparison of quenching by spin-labeled and brominated lipids. Biochemistry 31 (23):5312-5322
    • (1992) Biochemistry , vol.31 , Issue.23 , pp. 5312-5322
    • Abrams, F.S.1    London, E.2
  • 83
    • 0023652259 scopus 로고
    • Parallax method for direct measurement of membrane penetration depth utilizing fluorescence quenching by spin-labeled phospholipids
    • Chattopadhyay A, London E (1987) Parallax method for direct measurement of membrane penetration depth utilizing fluorescence quenching by spin-labeled phospholipids. Biochemistry 26 (1):39-45
    • (1987) Biochemistry , vol.26 , Issue.1 , pp. 39-45
    • Chattopadhyay, A.1    London, E.2
  • 84
    • 0025051457 scopus 로고
    • Quenching of tryptophan fluorescence by brominated phospholipid
    • Bolen EJ, Holloway PW (1990) Quenching of tryptophan fluorescence by brominated phospholipid. Biochemistry 29 (41):9638-9643
    • (1990) Biochemistry , vol.29 , Issue.41 , pp. 9638-9643
    • Bolen, E.J.1    Holloway, P.W.2
  • 85
    • 33846399142 scopus 로고    scopus 로고
    • E (z),a depthdependent potential for assessing the energies of insertion of amino acid side-chains into membranes: Derivation and applications to determining the orientation of transmembrane and interfacial helices
    • Senes A, Chadi DC, Law PB, Walters RF, Nanda V, Degrado WF (2007) E (z), a depthdependent potential for assessing the energies of insertion of amino acid side-chains into membranes: derivation and applications to determining the orientation of transmembrane and interfacial helices. J Mol Biol 366 (2):436-448
    • (2007) J Mol Biol , vol.366 , Issue.2 , pp. 436-448
    • Senes, A.1    Chadi, D.C.2    Law, P.B.3    Walters, R.F.4    Nanda, V.5    Degrado, W.F.6
  • 86
    • 84861038844 scopus 로고    scopus 로고
    • Knowledge-based potential for positioning membrane-associated structures and assessing residue-specific energetic contributions
    • doi: 10.1016/j.str.2012.03.016
    • Schramm CA, Hannigan BT, Donald JE, Keasar C, Saven JG, Degrado WF, Samish I (2012) Knowledge-based potential for positioning membrane-associated structures and assessing residue-specific energetic contributions. Structure 20 (5):924-935. doi: 10.1016/j.str.2012.03.016
    • (2012) Structure , vol.20 , Issue.5 , pp. 924-935
    • Schramm, C.A.1    Hannigan, B.T.2    Donald, J.E.3    Keasar, C.4    Saven, J.G.5    Degrado, W.F.6    Samish, I.7
  • 87
    • 0027499143 scopus 로고
    • Non-random distribution of amino acids in the transmembrane segments of human type i single span membrane proteins
    • doi: 10.1006/jmbi.1993.1066
    • Landolt-Marticorena C, Williams KA, Deber CM, Reithmeier RA (1993) Non-random distribution of amino acids in the transmembrane segments of human type I single span membrane proteins. J Mol Biol 229 (3): 602-608. doi: 10.1006/jmbi.1993.1066
    • (1993) J Mol Biol , vol.229 , Issue.3 , pp. 602-608
    • Landolt-Marticorena, C.1    Williams, K.A.2    Deber, C.M.3    Reithmeier, R.A.4
  • 88
    • 84857737028 scopus 로고    scopus 로고
    • Hydrophobic mismatch of mobile transmembrane helices: Merging theory and experiments
    • doi: 10.1016/j. bbamem.2012.01.023
    • Strandberg E, Esteban-Martin S, Ulrich AS, Salgado J (2012) Hydrophobic mismatch of mobile transmembrane helices: merging theory and experiments. Biochim Biophys Acta 1818 (5):1242-1249. doi: 10.1016/j. bbamem.2012.01.023
    • (2012) Biochim Biophys Acta , vol.1818 , Issue.5 , pp. 1242-1249
    • Strandberg, E.1    Esteban-Martin, S.2    Ulrich, A.S.3    Salgado, J.4
  • 89
    • 77952093470 scopus 로고    scopus 로고
    • Orientation and dynamics of transmembrane peptides: The power of simple models
    • doi: 10.1007/s00249-009-0567-1
    • Holt A, Killian JA (2010) Orientation and dynamics of transmembrane peptides: the power of simple models. Eur Biophys J 39 (4): 609-621. doi: 10.1007/s00249-009-0567-1
    • (2010) Eur Biophys J , vol.39 , Issue.4 , pp. 609-621
    • Holt, A.1    Killian, J.A.2
  • 90
    • 37049023237 scopus 로고    scopus 로고
    • On the orientation of a designed transmembrane peptide: Toward the right tilt angle?
    • doi: 10.1021/ja073784q
    • Ozdirekcan S, Etchebest C, Killian JA, Fuchs PF (2007) On the orientation of a designed transmembrane peptide: toward the right tilt angle? J Am Chem Soc 129 (49): 15174-15181. doi: 10.1021/ja073784q
    • (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.4
  • 91
    • 70350031590 scopus 로고    scopus 로고
    • Alamethicin aggregation in lipid membranes
    • doi: 10.1007/ s00232-009-9199-8
    • Pan J, Tristram-Nagle S, Nagle JF (2009) Alamethicin aggregation in lipid membranes. J Membr Biol 231 (1):11-27. doi: 10.1007/ s00232-009-9199-8
    • (2009) J Membr Biol , vol.231 , Issue.1 , pp. 11-27
    • Pan, J.1    Tristram-Nagle, S.2    Nagle, J.F.3
  • 92
    • 0242405501 scopus 로고    scopus 로고
    • Synthetic peptides as models for intrinsic membrane proteins
    • Killian JA (2003) Synthetic peptides as models for intrinsic membrane proteins. FEBS Lett 555 (1):134-138
    • (2003) FEBS Lett , vol.555 , Issue.1 , pp. 134-138
    • Killian, J.A.1
  • 93
    • 0242659352 scopus 로고    scopus 로고
    • Proteinlipid interactions studied with designed transmembrane peptides: Role of hydrophobic matching and interfacial anchoring
    • doi: 10.1080/09687680310001605352
    • de Planque MR, Killian JA (2003) Proteinlipid interactions studied with designed transmembrane peptides: role of hydrophobic matching and interfacial anchoring. Mol Membr Biol 20 (4):271-284. doi: 10.1080/0 9687680310001605352
    • (2003) Mol Membr Biol , vol.20 , Issue.4 , pp. 271-284
    • De Planque, M.R.1    Killian, J.A.2
  • 95
    • 44149116437 scopus 로고    scopus 로고
    • Effect of lipid composition on the topography of membrane- associated hydrophobic helices: Stabilization of transmembrane topography by anionic lipids
    • doi: 10.1016/j.jmb.2008.04.026
    • Shahidullah K, London E (2008) Effect of lipid composition on the topography of membrane- associated hydrophobic helices: stabilization of transmembrane topography by anionic lipids. J Mol Biol 379 (4):704-718. doi: 10.1016/j.jmb.2008.04.026
    • (2008) J Mol Biol , vol.379 , Issue.4 , pp. 704-718
    • Shahidullah, K.1    London, E.2
  • 96
    • 0017396567 scopus 로고
    • Vesicles of variable diameter prepared by a modified injection method
    • Kremer JM, Esker MW, Pathmamanoharan C, Wiersema PH (1977) Vesicles of variable diameter prepared by a modified injection method. Biochemistry 16 (17):3932-3935
    • (1977) Biochemistry , vol.16 , Issue.17 , pp. 3932-3935
    • Kremer, J.M.1    Esker, M.W.2    Pathmamanoharan, C.3    Wiersema, P.H.4
  • 97
    • 0017511458 scopus 로고
    • Dynamics of phospholipid aggregation in ethanol-water solutions
    • Aarts PA, Gijeman OL, Kremer JM, Wiersema PH (1977) Dynamics of phospholipid aggregation in ethanol-water solutions. Chem Phys Lipids 19 (3):267-274
    • (1977) Chem Phys Lipids , vol.19 , Issue.3 , pp. 267-274
    • Aarts, P.A.1    Gijeman, O.L.2    Kremer, J.M.3    Wiersema, P.H.4
  • 98
    • 34547640055 scopus 로고    scopus 로고
    • Using model membraneinserted hydrophobic helices to study the equilibrium between transmembrane and nontransmembrane states
    • London E (2007) Using model membraneinserted hydrophobic helices to study the equilibrium between transmembrane and nontransmembrane states. J Gen Physiol 130 (2): 229-232
    • (2007) J Gen Physiol , vol.130 , Issue.2 , pp. 229-232
    • London, E.1
  • 99
    • 74649085539 scopus 로고    scopus 로고
    • The effect of hydrophilic substitutions and anionic lipids upon the transverse positioning of the transmembrane helix of the ErbB2 (neu) protein incorporated into model membrane vesicles
    • doi: 10.1016/j.jmb.2009.11.037
    • Shahidullah K, Krishnakumar SS, London E (2010) The effect of hydrophilic substitutions and anionic lipids upon the transverse positioning of the transmembrane helix of the ErbB2 (neu) protein incorporated into model membrane vesicles. J Mol Biol 396 (1): 209-220. doi: 10.1016/j.jmb.2009.11.037
    • (2010) J Mol Biol , vol.396 , Issue.1 , pp. 209-220
    • Shahidullah, K.1    Krishnakumar, S.S.2    London, E.3
  • 100
    • 0028142681 scopus 로고
    • Effect of charged residue substitutions on the membrane- interactive properties of signal sequences of the Escherichia coli LamB protein
    • doi: 10.1016/ S0006-3495 (94)80627-7
    • Jones JD, Gierasch LM (1994) Effect of charged residue substitutions on the membrane- interactive properties of signal sequences of the Escherichia coli LamB protein. Biophys J 67 (4):1534-1545. doi: 10.1016/ S0006-3495 (94)80627-7
    • (1994) Biophys J , vol.67 , Issue.4 , pp. 1534-1545
    • Jones, J.D.1    Gierasch, L.M.2
  • 102
    • 0034672769 scopus 로고    scopus 로고
    • Small-angle neutron scattering study of the n-decane effect on the bilayer thickness in extruded unilamellar dioleoylphosphatidylcholine liposomes
    • Uhrikova D, Balgavy P, Kucerka N, Islamov A, Gordeliy V, Kuklin A (2000) Small-angle neutron scattering study of the n-decane effect on the bilayer thickness in extruded unilamellar dioleoylphosphatidylcholine liposomes. Biophys Chem 88 (1-3): 165-170
    • (2000) Biophys Chem , vol.88 , Issue.1-3 , pp. 165-170
    • Uhrikova, D.1    Balgavy, P.2    Kucerka, N.3    Islamov, A.4    Gordeliy, V.5    Kuklin, A.6
  • 103
    • 0026704101 scopus 로고
    • Combined influence of cholesterol and synthetic amphiphillic peptides upon bilayer thickness in model membranes
    • doi: 10.1016/S0006-3495 (92)81926-4
    • Nezil FA, Bloom M (1992) Combined influence of cholesterol and synthetic amphiphillic peptides upon bilayer thickness in model membranes. Biophys J 61 (5):1176-1183. doi: 10.1016/S0006-3495 (92)81926-4
    • (1992) Biophys J , vol.61 , Issue.5 , pp. 1176-1183
    • Nezil, F.A.1    Bloom, M.2
  • 104
    • 79953255545 scopus 로고    scopus 로고
    • Methyl-beta-cyclodextrins preferentially remove cholesterol from the liquid disordered phase in giant unilamellar vesicles
    • doi: 10.1007/ s00232-011-9348-8
    • Sanchez SA, Gunther G, Tricerri MA, Gratton E (2011) Methyl-beta- cyclodextrins preferentially remove cholesterol from the liquid disordered phase in giant unilamellar vesicles. J Membr Biol 241 (1):1-10. doi: 10.1007/ s00232-011-9348-8
    • (2011) J Membr Biol , vol.241 , Issue.1 , pp. 1-10
    • Sanchez, S.A.1    Gunther, G.2    Tricerri, M.A.3    Gratton, E.4
  • 105
    • 0242385346 scopus 로고    scopus 로고
    • Separation of liquid phases in giant vesicles of ternary mixtures of phospholipids and cholesterol
    • doi: 10.1016/ S0006-3495 (03)74726-2
    • Veatch SL, Keller SL (2003) Separation of liquid phases in giant vesicles of ternary mixtures of phospholipids and cholesterol. Biophys J 85 (5):3074-3083. doi: 10.1016/ S0006-3495 (03) 74726-2
    • (2003) Biophys J , vol.85 , Issue.5 , pp. 3074-3083
    • Veatch, S.L.1    Keller, S.L.2
  • 106
    • 49749131164 scopus 로고    scopus 로고
    • Computationally designed peptide inhibitors of proteinprotein interactions in membranes
    • doi: 10.1021/ bi800687h
    • Caputo GA, Litvinov RI, Li W, Bennett JS, Degrado WF, Yin H (2008) Computationally designed peptide inhibitors of proteinprotein interactions in membranes. Biochemistry 47 (33):8600-8606. doi: 10.1021/ bi800687h
    • (2008) Biochemistry , vol.47 , Issue.33 , pp. 8600-8606
    • Caputo, G.A.1    Litvinov, R.I.2    Li, W.3    Bennett, J.S.4    Degrado, W.F.5    Yin, H.6
  • 107
    • 13544273837 scopus 로고    scopus 로고
    • Topography of diphtheria toxin A chain inserted into lipid vesicles
    • Hayashibara M, London E (2005) Topography of diphtheria toxin A chain inserted into lipid vesicles. Biochemistry 44 (6): 2183-2196
    • (2005) Biochemistry , vol.44 , Issue.6 , pp. 2183-2196
    • Hayashibara, M.1    London, E.2
  • 108
    • 18244428625 scopus 로고    scopus 로고
    • Conformational adaptation of annexin v upon binding to liposomes: A time-resolved fluorescence study
    • doi: 10.1006/ bbrc.1997.6596
    • Follenius-Wund A, Piemont E, Freyssinet JM, Gerard D, Pigault C (1997) Conformational adaptation of annexin V upon binding to liposomes: a time-resolved fluorescence study. Biochem Biophys Res Commun 234 (1):111-116. doi: 10.1006/ bbrc.1997.6596
    • (1997) Biochem Biophys Res Commun , vol.234 , Issue.1 , pp. 111-116
    • Follenius-Wund, A.1    Piemont, E.2    Freyssinet, J.M.3    Gerard, D.4    Pigault, C.5


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