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Volumn 1848, Issue 1, 2015, Pages 246-259

Elastic deformation and area per lipid of membranes: Atomistic view from solid-state deuterium NMR spectroscopy

Author keywords

Area per lipid; Lipid protein interaction; Molecular dynamics; Order parameter; Osmotic pressure; Solid state NMR

Indexed keywords

G PROTEIN COUPLED RECEPTOR; DEUTERIUM; LIPID BILAYER;

EID: 84924336957     PISSN: 00052736     EISSN: 18792642     Source Type: Journal    
DOI: 10.1016/j.bbamem.2014.06.004     Document Type: Review
Times cited : (49)

References (140)
  • 1
    • 0000934428 scopus 로고
    • 14N quadrupolar relaxation
    • 14N quadrupolar relaxation J. Chem. Phys. 77 1982 1576 1599
    • (1982) J. Chem. Phys. , vol.77 , pp. 1576-1599
    • Brown, M.F.1
  • 2
    • 79957760088 scopus 로고    scopus 로고
    • 2H NMR relaxation illuminates functional dynamics of retinal cofactor in membrane activation of rhodopsin
    • 2H NMR relaxation illuminates functional dynamics of retinal cofactor in membrane activation of rhodopsin Proc. Natl. Acad. Sci. U. S. A. 108 2011 8263 8268
    • (2011) Proc. Natl. Acad. Sci. U. S. A. , vol.108 , pp. 8263-8268
    • Struts, A.V.1    Salgado, G.F.J.2    Brown, M.F.3
  • 4
    • 84870901092 scopus 로고    scopus 로고
    • Curvature forces in membrane lipid-protein interactions
    • M.F. Brown Curvature forces in membrane lipid-protein interactions Biochemistry 51 2012 9782 9795
    • (2012) Biochemistry , vol.51 , pp. 9782-9795
    • Brown, M.F.1
  • 5
    • 0036286853 scopus 로고    scopus 로고
    • Lipid bilayers, NMR relaxation, and computer simulations
    • R.W. Pastor, R.M. Venable, and S.E. Feller Lipid bilayers, NMR relaxation, and computer simulations Acc. Chem. Res. 35 2002 438 446
    • (2002) Acc. Chem. Res. , vol.35 , pp. 438-446
    • Pastor, R.W.1    Venable, R.M.2    Feller, S.E.3
  • 6
    • 79959741351 scopus 로고    scopus 로고
    • Interpretation of fluctuation spectra in lipid bilayer simulations
    • E.G. Brandt, A.R. Braun, J.N. Sachs, J.F. Nagle, and O. Edholm Interpretation of fluctuation spectra in lipid bilayer simulations Biophys. J. 100 2011 2104 2111
    • (2011) Biophys. J. , vol.100 , pp. 2104-2111
    • Brandt, E.G.1    Braun, A.R.2    Sachs, J.N.3    Nagle, J.F.4    Edholm, O.5
  • 7
    • 84878152855 scopus 로고    scopus 로고
    • Bending free energy from simulation: Correspondence of planar and inverse hexagonal lipid phases
    • A.J. Sodt, and R.W. Pastor Bending free energy from simulation: correspondence of planar and inverse hexagonal lipid phases Biophys. J. 104 2013 2202 2211
    • (2013) Biophys. J. , vol.104 , pp. 2202-2211
    • Sodt, A.J.1    Pastor, R.W.2
  • 10
    • 84861770615 scopus 로고    scopus 로고
    • Coarse-graining of multi-protein assemblies
    • M.G. Saunders, and G.A. Voth Coarse-graining of multi-protein assemblies Curr. Opin. Struct. Biol. 12 2012 144 150
    • (2012) Curr. Opin. Struct. Biol. , vol.12 , pp. 144-150
    • Saunders, M.G.1    Voth, G.A.2
  • 12
    • 49549083949 scopus 로고    scopus 로고
    • Membrane proteins: Molecular dynamics simulations
    • E. Lindahl, and M.S.P. Sansom Membrane proteins: molecular dynamics simulations Curr. Opin. Struct. Biol. 18 2008 425 431
    • (2008) Curr. Opin. Struct. Biol. , vol.18 , pp. 425-431
    • Lindahl, E.1    Sansom, M.S.P.2
  • 13
    • 0035395820 scopus 로고    scopus 로고
    • Composite membrane deformation on the mesoscopic length scale
    • 010901-1-010901-4
    • M.F. Brown, R.L. Thurmond, S.W. Dodd, D. Otten, and K. Beyer Composite membrane deformation on the mesoscopic length scale Phys. Rev. E. 64 2001 010901-1-010901-4
    • (2001) Phys. Rev. E. , vol.64
    • Brown, M.F.1    Thurmond, R.L.2    Dodd, S.W.3    Otten, D.4    Beyer, K.5
  • 15
    • 0017672468 scopus 로고
    • Ion-induced changes in head group conformation of lecithin bilayers
    • M.F. Brown, and J. Seelig Ion-induced changes in head group conformation of lecithin bilayers Nature 269 1977 721 723
    • (1977) Nature , vol.269 , pp. 721-723
    • Brown, M.F.1    Seelig, J.2
  • 16
  • 18
    • 66249083118 scopus 로고    scopus 로고
    • Emerging roles for lipids in shaping membrane-protein function
    • R. Phillips, T. Ursell, P. Wiggins, and P. Sens Emerging roles for lipids in shaping membrane-protein function Nature 459 2009 379 385
    • (2009) Nature , vol.459 , pp. 379-385
    • Phillips, R.1    Ursell, T.2    Wiggins, P.3    Sens, P.4
  • 19
    • 33845505655 scopus 로고    scopus 로고
    • Curvature and hydrophobic forces drive constitutive association and modulate activity of rhodopsin in membranes
    • A.V. Botelho, T. Huber, T.P. Sakmar, and M.F. Brown Curvature and hydrophobic forces drive constitutive association and modulate activity of rhodopsin in membranes Biophys. J. 91 2006 4464 4477
    • (2006) Biophys. J. , vol.91 , pp. 4464-4477
    • Botelho, A.V.1    Huber, T.2    Sakmar, T.P.3    Brown, M.F.4
  • 20
    • 0028124422 scopus 로고
    • Modulation of rhodopsin function by properties of the membrane bilayer
    • M.F. Brown Modulation of rhodopsin function by properties of the membrane bilayer Chem. Phys. Lipids 73 1994 159 180
    • (1994) Chem. Phys. Lipids , vol.73 , pp. 159-180
    • Brown, M.F.1
  • 21
    • 44949153462 scopus 로고    scopus 로고
    • Collective and noncollective models of NMR relaxation in lipid vesicles and multilayers
    • J.B. Klauda, N.V. Eldho, K. Gawrisch, B.R. Brooks, and R.W. Pastor Collective and noncollective models of NMR relaxation in lipid vesicles and multilayers J. Phys. Chem. B 112 2008 5924 5929
    • (2008) J. Phys. Chem. B , vol.112 , pp. 5924-5929
    • Klauda, J.B.1    Eldho, N.V.2    Gawrisch, K.3    Brooks, B.R.4    Pastor, R.W.5
  • 23
    • 77249112159 scopus 로고    scopus 로고
    • Comparative analysis of membrane-associated fusion peptide secondary structure and lipid mixing function of HIV gp41 constructs that model the early pre-hairpin intermediate and final hairpin conformations
    • K. Sackett, M.J. Nethercott, R.F. Epand, R.M. Epand, D.R. Kindra, Y. Shai, and D.P. Weliky Comparative analysis of membrane-associated fusion peptide secondary structure and lipid mixing function of HIV gp41 constructs that model the early pre-hairpin intermediate and final hairpin conformations J. Mol. Biol. 397 2010 301 315
    • (2010) J. Mol. Biol. , vol.397 , pp. 301-315
    • Sackett, K.1    Nethercott, M.J.2    Epand, R.F.3    Epand, R.M.4    Kindra, D.R.5    Shai, Y.6    Weliky, D.P.7
  • 25
    • 84859912916 scopus 로고    scopus 로고
    • Membrane protein structure and dynamics from NMR spectroscopy
    • M. Hong, Y. Zhang, and F. Hu Membrane protein structure and dynamics from NMR spectroscopy Annu. Rev. Phys. Chem. 63 2012 1 24
    • (2012) Annu. Rev. Phys. Chem. , vol.63 , pp. 1-24
    • Hong, M.1    Zhang, Y.2    Hu, F.3
  • 26
    • 85036363664 scopus 로고    scopus 로고
    • Pressure-induced ordering in mixed-lipid bilayers
    • 011913-1-011913-9
    • A. Brown, I. Skanes, and M.R. Morrow Pressure-induced ordering in mixed-lipid bilayers Phys. Rev. E. 2004 011913-1-011913-9
    • (2004) Phys. Rev. E.
    • Brown, A.1    Skanes, I.2    Morrow, M.R.3
  • 27
    • 67650285019 scopus 로고    scopus 로고
    • Structure and dynamics of membrane proteins by magic angle spinning solid-state NMR
    • A. McDermott Structure and dynamics of membrane proteins by magic angle spinning solid-state NMR Annu. Rev. Biophys. 38 2009 385 403
    • (2009) Annu. Rev. Biophys. , vol.38 , pp. 385-403
    • McDermott, A.1
  • 28
    • 77953065253 scopus 로고    scopus 로고
    • Structural dynamics of bio-macromolecules by NMR: The slowly relaxing local structure approach
    • E. Meirovitch, Y.E. Shapiro, A. Polimeno, and J.H. Freed Structural dynamics of bio-macromolecules by NMR: the slowly relaxing local structure approach Prog. Nucl. Magn. Reson. Spectrosc. 56 2010 360 405
    • (2010) Prog. Nucl. Magn. Reson. Spectrosc. , vol.56 , pp. 360-405
    • Meirovitch, E.1    Shapiro, Y.E.2    Polimeno, A.3    Freed, J.H.4
  • 29
    • 79952361482 scopus 로고    scopus 로고
    • Retinal dynamics underlie its switch from inverse agonist to agonist during rhodopsin activation
    • A.V. Struts, G.F.J. Salgado, K. Martínez-Mayorga, and M.F. Brown Retinal dynamics underlie its switch from inverse agonist to agonist during rhodopsin activation Nat. Struct. Mol. Biol. 18 2011 392 394
    • (2011) Nat. Struct. Mol. Biol. , vol.18 , pp. 392-394
    • Struts, A.V.1    Salgado, G.F.J.2    Martínez-Mayorga, K.3    Brown, M.F.4
  • 30
    • 84886720456 scopus 로고    scopus 로고
    • Sum of the parts: Composition and architecture of the bacterial extracellular matrix
    • O.A. McCrate, X. Zhou, C. Reichhardt, and L. Cegelski Sum of the parts: composition and architecture of the bacterial extracellular matrix J. Mol. Biol. 425 2013 4286 4294
    • (2013) J. Mol. Biol. , vol.425 , pp. 4286-4294
    • McCrate, O.A.1    Zhou, X.2    Reichhardt, C.3    Cegelski, L.4
  • 32
    • 33750239249 scopus 로고    scopus 로고
    • The physical chemistry of biological membranes
    • J. Zimmerberg, and K. Gawrisch The physical chemistry of biological membranes Nat. Chem. Biol. 2 2006 564 567
    • (2006) Nat. Chem. Biol. , vol.2 , pp. 564-567
    • Zimmerberg, J.1    Gawrisch, K.2
  • 36
    • 3142543171 scopus 로고    scopus 로고
    • Perturbation of the hydrophobic core of lipid bilayers by the human antimicrobial peptide LL-37
    • K.A. Henzler-Wildman, G.V. Martinez, M.F. Brown, and A. Ramamoorthy Perturbation of the hydrophobic core of lipid bilayers by the human antimicrobial peptide LL-37 Biochemistry 43 2004 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
  • 37
    • 0037150089 scopus 로고    scopus 로고
    • Conformational energetics of rhodopsin modulated by nonlamellar forming lipids
    • A.V. Botelho, N.J. Gibson, Y. Wang, R.L. Thurmond, and M.F. Brown Conformational energetics of rhodopsin modulated by nonlamellar forming lipids Biochemistry 41 2002 6354 6368
    • (2002) Biochemistry , vol.41 , pp. 6354-6368
    • Botelho, A.V.1    Gibson, N.J.2    Wang, Y.3    Thurmond, R.L.4    Brown, M.F.5
  • 39
    • 0037014696 scopus 로고    scopus 로고
    • Electrostatic properties of membrane lipids coupled to metarhodopsin II formation in visual transduction
    • Y. Wang, A.V. Botelho, G.V. Martinez, and M.F. Brown Electrostatic properties of membrane lipids coupled to metarhodopsin II formation in visual transduction J. Am. Chem. Soc. 124 2002 7690 7701
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 7690-7701
    • Wang, Y.1    Botelho, A.V.2    Martinez, G.V.3    Brown, M.F.4
  • 40
    • 0036725152 scopus 로고    scopus 로고
    • Physical principles underlying the transduction of bilayer deformation forces during mechanosensitive channel gating
    • E. Perozo, A. Kloda, D.M. Cortes, and B. Martinac Physical principles underlying the transduction of bilayer deformation forces during mechanosensitive channel gating Nat. Struct. Biol. 9 2002 696 703
    • (2002) Nat. Struct. Biol. , vol.9 , pp. 696-703
    • Perozo, E.1    Kloda, A.2    Cortes, D.M.3    Martinac, B.4
  • 42
    • 33845901815 scopus 로고    scopus 로고
    • Lipid rafts: At a crossroad between cell biology and physics
    • K. Jacobson, O.G. Mouritsen, and R.G.W. Anderson Lipid rafts: at a crossroad between cell biology and physics Nat. Cell Biol. 9 2007 7 14
    • (2007) Nat. Cell Biol. , vol.9 , pp. 7-14
    • Jacobson, K.1    Mouritsen, O.G.2    Anderson, R.G.W.3
  • 43
    • 0027360175 scopus 로고
    • High-resolution conformation of gramicidin A in a lipid bilayer by solid-state NMR
    • R.R. Ketchem, W. Hu, and T.A. Cross High-resolution conformation of gramicidin A in a lipid bilayer by solid-state NMR Science 261 1993 1457 1460
    • (1993) Science , vol.261 , pp. 1457-1460
    • Ketchem, R.R.1    Hu, W.2    Cross, T.A.3
  • 44
    • 34347262391 scopus 로고    scopus 로고
    • Bilayer thickness and membrane protein function: An energetic perspective
    • O.S. Andersen, and R.E. Koeppe II Bilayer thickness and membrane protein function: an energetic perspective Annu. Rev. Biophys. Bioeng. 36 2007 107 130
    • (2007) Annu. Rev. Biophys. Bioeng. , vol.36 , pp. 107-130
    • Andersen, O.S.1    Koeppe, I.I.R.E.2
  • 45
    • 7044241302 scopus 로고    scopus 로고
    • How lipids affect the activities of integral membrane proteins
    • A.G. Lee How lipids affect the activities of integral membrane proteins Biochim. Biophys. Acta 1666 2004 62 87
    • (2004) Biochim. Biophys. Acta , vol.1666 , pp. 62-87
    • Lee, A.G.1
  • 48
    • 0030771815 scopus 로고    scopus 로고
    • Membrane lateral compressibility determined by NMR and X-ray diffraction: Effect of acyl chain polyunsaturation
    • B. Koenig, H. Strey, and K. Gawrisch Membrane lateral compressibility determined by NMR and X-ray diffraction: effect of acyl chain polyunsaturation Biophys. J. 73 1997 1954 1966
    • (1997) Biophys. J. , vol.73 , pp. 1954-1966
    • Koenig, B.1    Strey, H.2    Gawrisch, K.3
  • 49
    • 0023658631 scopus 로고
    • Steric repulsion between phosphatidylcholine bilayers
    • T.J. McIntosh, A.D. Magid, and S.A. Simon Steric repulsion between phosphatidylcholine bilayers Biochemistry 26 1987 7325 7332
    • (1987) Biochemistry , vol.26 , pp. 7325-7332
    • McIntosh, T.J.1    Magid, A.D.2    Simon, S.A.3
  • 51
    • 2942675244 scopus 로고    scopus 로고
    • Lipid bilayer pressure profiles and mechanosensitive channel gating
    • J. Gullingsrud, and K. Schulten Lipid bilayer pressure profiles and mechanosensitive channel gating Biophys. J. 86 2004 3496 3509
    • (2004) Biophys. J. , vol.86 , pp. 3496-3509
    • Gullingsrud, J.1    Schulten, K.2
  • 52
    • 0037134267 scopus 로고    scopus 로고
    • Control of the selectivity of the aquaporin water channel family by global orientational tuning
    • E. Tajkhorshid, P. Nollert, M.∅. Jensen, L.J.W. Miercke, J. O'Connell, R.M. Stroud, and K. Schulten Control of the selectivity of the aquaporin water channel family by global orientational tuning Science 296 2002 525 530
    • (2002) Science , vol.296 , pp. 525-530
    • Tajkhorshid, E.1    Nollert, P.2    Miercke, L.J.W.3    O'Connell, J.4    Stroud, R.M.5    Schulten, K.6
  • 53
    • 36449007836 scopus 로고
    • Constant pressure molecular dynamics simulation: The Langevin piston method
    • S.E. Feller, Y.H. Zhang, R.W. Pastor, and B.R. Brooks Constant pressure molecular dynamics simulation: the Langevin piston method J. Chem. Phys. 103 1995 4613 4621
    • (1995) J. Chem. Phys. , vol.103 , pp. 4613-4621
    • Feller, S.E.1    Zhang, Y.H.2    Pastor, R.W.3    Brooks, B.R.4
  • 54
    • 84861830828 scopus 로고    scopus 로고
    • Effect of membrane tension on the physical properties of DOPC lipid bilayer membrane
    • A.S. Reddy, D.T. Warshaviak, and M. Chachisvilis Effect of membrane tension on the physical properties of DOPC lipid bilayer membrane Biochim. Biophys. Acta 1818 2012 2271 2281
    • (2012) Biochim. Biophys. Acta , vol.1818 , pp. 2271-2281
    • Reddy, A.S.1    Warshaviak, D.T.2    Chachisvilis, M.3
  • 55
    • 0000386579 scopus 로고
    • The ordering of water and its relation to the hydration force
    • S.-J. Marrink, M. Berkowitz, and H.J. Berendsen The ordering of water and its relation to the hydration force Langmuir 9 1993 3122 3131
    • (1993) Langmuir , vol.9 , pp. 3122-3131
    • Marrink, S.-J.1    Berkowitz, M.2    Berendsen, H.J.3
  • 56
    • 33750037303 scopus 로고    scopus 로고
    • Direct observation of Bin/amphiphysin/Rvs (BAR) domain-induced membrane curvature by means of molecular dynamics simulations
    • P.D. Blood, and G.A. Voth Direct observation of Bin/amphiphysin/Rvs (BAR) domain-induced membrane curvature by means of molecular dynamics simulations Proc. Natl. Acad. Sci. U. S. A. 103 2006 15068 15072
    • (2006) Proc. Natl. Acad. Sci. U. S. A. , vol.103 , pp. 15068-15072
    • Blood, P.D.1    Voth, G.A.2
  • 57
    • 51649170084 scopus 로고
    • Undulations, steric interaction and cohesion of fluid membranes
    • W. Helfrich, and R.-M. Servuss Undulations, steric interaction and cohesion of fluid membranes Nuovo Cimento Soc. Ital. Fis., D 3 1984 137 151
    • (1984) Nuovo Cimento Soc. Ital. Fis., D , vol.3 , pp. 137-151
    • Helfrich, W.1    Servuss, R.-M.2
  • 58
    • 0033932837 scopus 로고    scopus 로고
    • Effect of chain length and unsaturation on elasticity of lipid bilayers
    • W. Rawicz, K.C. Olbrich, T. McIntosh, D. Needham, and E. Evans Effect of chain length and unsaturation on elasticity of lipid bilayers Biophys. J. 79 2000 328 339
    • (2000) Biophys. J. , vol.79 , pp. 328-339
    • Rawicz, W.1    Olbrich, K.C.2    McIntosh, T.3    Needham, D.4    Evans, E.5
  • 59
    • 33745041479 scopus 로고    scopus 로고
    • Roles of bilayer material properties in function and distribution of membrane proteins
    • T.J. McIntosh, and S.A. Simon Roles of bilayer material properties in function and distribution of membrane proteins Annu. Rev. Biophys. Biomol. Struct. 35 2006 177 198
    • (2006) Annu. Rev. Biophys. Biomol. Struct. , vol.35 , pp. 177-198
    • McIntosh, T.J.1    Simon, S.A.2
  • 60
    • 26944481188 scopus 로고    scopus 로고
    • Interfaces and the driving force of hydrophobic assembly
    • D. Chandler Interfaces and the driving force of hydrophobic assembly Nature 437 2005 640 647
    • (2005) Nature , vol.437 , pp. 640-647
    • Chandler, D.1
  • 62
    • 0034257990 scopus 로고    scopus 로고
    • Structural information from multilamellar liposomes at full hydration: Full q-range fitting with high quality x-ray data
    • G. Pabst, M. Rappolt, H. Amenitsch, and P. Laggner Structural information from multilamellar liposomes at full hydration: full q-range fitting with high quality x-ray data Phys. Rev. E. 62 2000 4000 4009
    • (2000) Phys. Rev. E. , vol.62 , pp. 4000-4009
    • Pabst, G.1    Rappolt, M.2    Amenitsch, H.3    Laggner, P.4
  • 63
    • 0022512564 scopus 로고
    • Hydration force and bilayer deformation: A reevaluation
    • T.J. McIntosh, and S.A. Simon Hydration force and bilayer deformation: a reevaluation Biochemistry 25 1986 4058 4066
    • (1986) Biochemistry , vol.25 , pp. 4058-4066
    • McIntosh, T.J.1    Simon, S.A.2
  • 64
    • 0036179253 scopus 로고    scopus 로고
    • Comparative physiology of salt and water stress
    • R. Munns Comparative physiology of salt and water stress Plant Cell Environ. 25 2002 239 250
    • (2002) Plant Cell Environ. , vol.25 , pp. 239-250
    • Munns, R.1
  • 65
    • 0035825634 scopus 로고    scopus 로고
    • The gating mechanism of the large mechanosensitive channel Mscl
    • S. Sukharev, M. Betanzos, C.-S. Chiang, and H.R. Guy The gating mechanism of the large mechanosensitive channel Mscl Nature 409 2001 720 724
    • (2001) Nature , vol.409 , pp. 720-724
    • Sukharev, S.1    Betanzos, M.2    Chiang, C.-S.3    Guy, H.R.4
  • 67
    • 0034088841 scopus 로고    scopus 로고
    • Effect of ethanol and osmotic stress on receptor conformation. Reduced water activity amplifies the effect of ethanol on metarhodopsin II formation
    • D.C. Mitchell, and B.J. Litman Effect of ethanol and osmotic stress on receptor conformation. Reduced water activity amplifies the effect of ethanol on metarhodopsin II formation J. Biol. Chem. 275 2000 5355 5360
    • (2000) J. Biol. Chem. , vol.275 , pp. 5355-5360
    • Mitchell, D.C.1    Litman, B.J.2
  • 68
    • 36549051639 scopus 로고    scopus 로고
    • Measurement of lipid forces by X-ray diffraction and osmotic stress
    • A.M. Dopico, Humana press Totowa
    • H.I. Petrache, D. Harries, and V.A. Parsegian Measurement of lipid forces by X-ray diffraction and osmotic stress A.M. Dopico, Methods in Molecular Biology vol. 400 2007 Humana press Totowa 405 420
    • (2007) Methods in Molecular Biology , vol.400 VOL. , pp. 405-420
    • Petrache, H.I.1    Harries, D.2    Parsegian, V.A.3
  • 70
    • 0033944497 scopus 로고    scopus 로고
    • Short-range interactions between lipid bilayers measured by X-ray diffraction
    • T.J. McIntosh Short-range interactions between lipid bilayers measured by X-ray diffraction Curr. Opin. Struct. Biol. 10 2000 481 485
    • (2000) Curr. Opin. Struct. Biol. , vol.10 , pp. 481-485
    • McIntosh, T.J.1
  • 71
    • 0002787636 scopus 로고
    • X-ray diffraction studies of lipid-water systems
    • D. Chapman, Academic Press New York
    • V. Luzzati X-ray diffraction studies of lipid-water systems D. Chapman, Biological Membranes vol. 1 1968 Academic Press New York 71 123
    • (1968) Biological Membranes , vol.1 VOL. , pp. 71-123
    • Luzzati, V.1
  • 72
    • 0032987478 scopus 로고    scopus 로고
    • Membrane protein folding and stability: Physical principles
    • S.H. White, and W.C. Wimley Membrane protein folding and stability: physical principles Annu. Rev. Biophys. Biomol. Struct. 28 1999 319 365
    • (1999) Annu. Rev. Biophys. Biomol. Struct. , vol.28 , pp. 319-365
    • White, S.H.1    Wimley, W.C.2
  • 73
    • 0037763992 scopus 로고    scopus 로고
    • Collective chain dynamics in lipid bilayers by inelastic X-ray scattering
    • T.M. Weiss, P.J. Chen, H. Sinn, E.E. Alp, S.H. Chen, and H.W. Huang Collective chain dynamics in lipid bilayers by inelastic X-ray scattering Biophys. J. 84 2003 3767 3776
    • (2003) Biophys. J. , vol.84 , pp. 3767-3776
    • Weiss, T.M.1    Chen, P.J.2    Sinn, H.3    Alp, E.E.4    Chen, S.H.5    Huang, H.W.6
  • 74
    • 0017927954 scopus 로고
    • Neutron diffraction studies on selectively deuterated phospholipid bilayers
    • G. Büldt, H.U. Gally, A. Seelig, J. Seelig, and G. Zaccai Neutron diffraction studies on selectively deuterated phospholipid bilayers Nature 271 1978 182 184
    • (1978) Nature , vol.271 , pp. 182-184
    • Büldt, G.1    Gally, H.U.2    Seelig, A.3    Seelig, J.4    Zaccai, G.5
  • 75
    • 0029003107 scopus 로고
    • The potential and limitations of neutrons, electrons and X-rays for atomic-resolution microscopy of unstained biological molecules
    • R. Henderson The potential and limitations of neutrons, electrons and X-rays for atomic-resolution microscopy of unstained biological molecules Q. Rev. Biophys. 28 1995 171 193
    • (1995) Q. Rev. Biophys. , vol.28 , pp. 171-193
    • Henderson, R.1
  • 76
    • 36549002676 scopus 로고    scopus 로고
    • X-ray scattering and solid state deuterium nuclear magnetic resonance probes of structural fluctuations in lipid membranes
    • A.M. Dopico, Humana press Totowa
    • H.I. Petrache, and M.F. Brown X-ray scattering and solid state deuterium nuclear magnetic resonance probes of structural fluctuations in lipid membranes A.M. Dopico, Methods in Molecular Biology vol. 400 2007 Humana press Totowa 341 353
    • (2007) Methods in Molecular Biology , vol.400 VOL. , pp. 341-353
    • Petrache, H.I.1    Brown, M.F.2
  • 77
    • 0031824356 scopus 로고    scopus 로고
    • Structure and interactions of fully hydrated dioleoylphosphatidylcholine bilayers
    • S. Tristram-Nagle, H.I. Petrache, and J.F. Nagle Structure and interactions of fully hydrated dioleoylphosphatidylcholine bilayers Biophys. J. 75 1998 917 925
    • (1998) Biophys. J. , vol.75 , pp. 917-925
    • Tristram-Nagle, S.1    Petrache, H.I.2    Nagle, J.F.3
  • 78
    • 0026635481 scopus 로고
    • Membrane dipole potentials, hydration forces, and the ordering of water at membrane surfaces
    • K. Gawrisch, D. Ruston, J. Zimmerberg, V.A. Parsegian, R.P. Rand, and N.L. Fuller Membrane dipole potentials, hydration forces, and the ordering of water at membrane surfaces Biophys. J. 61 1992 1213 1223
    • (1992) Biophys. J. , vol.61 , pp. 1213-1223
    • Gawrisch, K.1    Ruston, D.2    Zimmerberg, J.3    Parsegian, V.A.4    Rand, R.P.5    Fuller, N.L.6
  • 80
    • 0016283654 scopus 로고
    • The dynamic structure of fatty acyl chains in a phospholipid bilayer measured by deuterium magnetic resonance
    • A. Seelig, and J. Seelig The dynamic structure of fatty acyl chains in a phospholipid bilayer measured by deuterium magnetic resonance Biochemistry 13 1974 4839 4845
    • (1974) Biochemistry , vol.13 , pp. 4839-4845
    • Seelig, A.1    Seelig, J.2
  • 81
    • 0001008704 scopus 로고
    • Molecular dynamics simulation of a bilayer of 200 lipids in the gel and in the liquid crystal phase
    • H. Heller, K. Schaefer, and K. Schulten Molecular dynamics simulation of a bilayer of 200 lipids in the gel and in the liquid crystal phase J. Phys. Chem. 97 1993 8343 8360
    • (1993) J. Phys. Chem. , vol.97 , pp. 8343-8360
    • Heller, H.1    Schaefer, K.2    Schulten, K.3
  • 82
    • 84865974865 scopus 로고    scopus 로고
    • Hydration repulsion between biomembranes results from an interplay of dehydration and depolarization
    • E. Schneck, F. Sedlmeier, and R.R. Netz Hydration repulsion between biomembranes results from an interplay of dehydration and depolarization Proc. Natl. Acad. Sci. U. S. A. 109 2012 14405 14409
    • (2012) Proc. Natl. Acad. Sci. U. S. A. , vol.109 , pp. 14405-14409
    • Schneck, E.1    Sedlmeier, F.2    Netz, R.R.3
  • 83
    • 33644989063 scopus 로고    scopus 로고
    • Computer simulation of proton solvation and transport in aqueous and biomolecular systems
    • G.A. Voth Computer simulation of proton solvation and transport in aqueous and biomolecular systems Acc. Chem. Res. 2006 143 150
    • (2006) Acc. Chem. Res. , pp. 143-150
    • Voth, G.A.1
  • 85
    • 0023057572 scopus 로고
    • Area per molecule and distribution of water in fully hydrated dilauroylphosphatidylethanolamine bilayers
    • T.J. McIntosh, and S.A. Simon Area per molecule and distribution of water in fully hydrated dilauroylphosphatidylethanolamine bilayers Biochemistry 25 1986 4948 4952
    • (1986) Biochemistry , vol.25 , pp. 4948-4952
    • McIntosh, T.J.1    Simon, S.A.2
  • 86
    • 33746897341 scopus 로고    scopus 로고
    • A molecular dynamics investigation of the influence of hydration and temperature
    • C.J. Hogberg, and A.P. Lyubartsev A molecular dynamics investigation of the influence of hydration and temperature J. Phys. Chem. B 110 2006 14326 14336
    • (2006) J. Phys. Chem. B , vol.110 , pp. 14326-14336
    • Hogberg, C.J.1    Lyubartsev, A.P.2
  • 87
    • 0029074355 scopus 로고
    • Hydration and order in lipid bilayers
    • C. Ho, S.J. Slater, and C.D. Stubbs Hydration and order in lipid bilayers Biochemistry 34 1995 6188 6195
    • (1995) Biochemistry , vol.34 , pp. 6188-6195
    • Ho, C.1    Slater, S.J.2    Stubbs, C.D.3
  • 88
    • 0023423499 scopus 로고
    • Partial specific volumes of lipid and water in mixtures of egg lecithin and water
    • S.H. White, R.E. Jacobs, and G.I. King Partial specific volumes of lipid and water in mixtures of egg lecithin and water Biophys. J. 52 1987 663 665
    • (1987) Biophys. J. , vol.52 , pp. 663-665
    • White, S.H.1    Jacobs, R.E.2    King, G.I.3
  • 90
    • 0027251833 scopus 로고
    • Area/lipid of bilayers from NMR
    • J.F. Nagle Area/lipid of bilayers from NMR Biophys. J. 64 1993 1476 1481
    • (1993) Biophys. J. , vol.64 , pp. 1476-1481
    • Nagle, J.F.1
  • 91
    • 0025134135 scopus 로고
    • II) phase, and non-lamellar phase transitions of lipids
    • II) phase, and non-lamellar phase transitions of lipids Biochim. Biophys. Acta 1031 1990 1 69
    • (1990) Biochim. Biophys. Acta , vol.1031 , pp. 1-69
    • Seddon, J.M.1
  • 92
    • 0011847313 scopus 로고
    • Stability of lyotropic phases with curved interfaces
    • S.M. Gruner Stability of lyotropic phases with curved interfaces J. Phys. Chem. 93 1989 7562 7570
    • (1989) J. Phys. Chem. , vol.93 , pp. 7562-7570
    • Gruner, S.M.1
  • 93
    • 0018792901 scopus 로고
    • Neutron diffraction studies on phosphatidylcholine model membranes: Head group conformation
    • G. Büldt, H.U. Gally, J. Seelig, and G. Zaccai Neutron diffraction studies on phosphatidylcholine model membranes: head group conformation J. Mol. Biol. 134 1979 673 691
    • (1979) J. Mol. Biol. , vol.134 , pp. 673-691
    • Büldt, G.1    Gally, H.U.2    Seelig, J.3    Zaccai, G.4
  • 95
    • 0001231454 scopus 로고
    • Structural dynamics in phospholipid bilayers from deuterium spin-lattice relaxation time measurements
    • M.F. Brown, J. Seelig, and U. Häberlen Structural dynamics in phospholipid bilayers from deuterium spin-lattice relaxation time measurements J. Chem. Phys. 70 1979 5045 5053
    • (1979) J. Chem. Phys. , vol.70 , pp. 5045-5053
    • Brown, M.F.1    Seelig, J.2    Häberlen, U.3
  • 97
    • 0017881605 scopus 로고
    • Lecithin bilayers. Density measurements and molecular interactions
    • J.F. Nagle, and D.A. Wilkinson Lecithin bilayers. Density measurements and molecular interactions Biophys. J. 23 1978 159 175
    • (1978) Biophys. J. , vol.23 , pp. 159-175
    • Nagle, J.F.1    Wilkinson, D.A.2
  • 98
    • 0030933013 scopus 로고    scopus 로고
    • Determination of component volumes of lipid bilayers from simulations
    • H.I. Petrache, S.E. Feller, and J.F. Nagle Determination of component volumes of lipid bilayers from simulations Biophys. J. 72 1997 2237 2242
    • (1997) Biophys. J. , vol.72 , pp. 2237-2242
    • Petrache, H.I.1    Feller, S.E.2    Nagle, J.F.3
  • 99
    • 0031820877 scopus 로고    scopus 로고
    • Phospholipid component volumes: Determination and application to bilayer structure calculations
    • R.S. Armen, O.D. Uitto, and S.E. Feller Phospholipid component volumes: determination and application to bilayer structure calculations Biophys. J. 75 1998 734 744
    • (1998) Biophys. J. , vol.75 , pp. 734-744
    • Armen, R.S.1    Uitto, O.D.2    Feller, S.E.3
  • 100
    • 0025925134 scopus 로고
    • 2H NMR spectroscopy of phospholipid bilayers containing docosahexaenoyl (22:6ω3) chains
    • 2H NMR spectroscopy of phospholipid bilayers containing docosahexaenoyl (22:6ω3) chains Biochemistry 30 1991 8386 8394
    • (1991) Biochemistry , vol.30 , pp. 8386-8394
    • Barry, J.A.1    Trouard, T.P.2    Salmon, A.3    Brown, M.F.4
  • 102
    • 0032990614 scopus 로고    scopus 로고
    • Analysis of simulated NMR order parameters for lipid bilayer structure determination
    • H.I. Petrache, K. Tu, and J.F. Nagle Analysis of simulated NMR order parameters for lipid bilayer structure determination Biophys. J. 76 1999 2479 2487
    • (1999) Biophys. J. , vol.76 , pp. 2479-2487
    • Petrache, H.I.1    Tu, K.2    Nagle, J.F.3
  • 103
    • 0024378918 scopus 로고
    • Hydration forces between phospholipid bilayers
    • R.P. Rand, and V.A. Parsegian Hydration forces between phospholipid bilayers Biochim. Biophys. Acta 988 1989 351 376
    • (1989) Biochim. Biophys. Acta , vol.988 , pp. 351-376
    • Rand, R.P.1    Parsegian, V.A.2
  • 104
    • 0011724892 scopus 로고
    • Dispersion interaction of crossed mica cylinders: A reanalysis of the Israelachvili-Tabor experiments
    • L.R. White, J.N. Israelachvili, and B.W. Ninham Dispersion interaction of crossed mica cylinders: a reanalysis of the Israelachvili-Tabor experiments J. Chem. Soc. Faraday Trans. 1 72 1976 2526 2536
    • (1976) J. Chem. Soc. Faraday Trans. 1 , vol.72 , pp. 2526-2536
    • White, L.R.1    Israelachvili, J.N.2    Ninham, B.W.3
  • 105
    • 33845281853 scopus 로고
    • Physical properties of surfactant bilayer membranes: Thermal transitions, elasticity, rigidity, cohesion and colloidal interactions
    • E. Evans, and D. Needham Physical properties of surfactant bilayer membranes: thermal transitions, elasticity, rigidity, cohesion and colloidal interactions J. Phys. Chem. 91 1987 4219 4228
    • (1987) J. Phys. Chem. , vol.91 , pp. 4219-4228
    • Evans, E.1    Needham, D.2
  • 106
  • 108
    • 11644275374 scopus 로고
    • Ion binding in amphiphile water systems. A comparison between electrostatic theories and NMR experiments
    • J.P. Fraissard, H.A. Resing, D. Reidel Publ. Co. Dordrecht
    • H. Wennerström, B. Lindman, S. Engström, O. Söderman, G. Lindblom, and G.J.T. Tiddy Ion binding in amphiphile water systems. A comparison between electrostatic theories and NMR experiments J.P. Fraissard, H.A. Resing, Magnetic Resonance in Colloid and Interface Science 1980 D. Reidel Publ. Co. Dordrecht 609 614
    • (1980) Magnetic Resonance in Colloid and Interface Science , pp. 609-614
    • Wennerström, H.1    Lindman, B.2    Engström, S.3    Söderman, O.4    Lindblom, G.5    Tiddy, G.J.T.6
  • 109
    • 85152344390 scopus 로고    scopus 로고
    • The forces between interacting bilayer membranes and the hydration of phospholipid assemblies
    • P.L. Yeagle, 2nd ed. CRC Press Boca Raton
    • R.P. Rand, and V.A. Parsegian The forces between interacting bilayer membranes and the hydration of phospholipid assemblies P.L. Yeagle, The Structure of Biological Membranes 2nd ed. 2004 CRC Press Boca Raton 201 241
    • (2004) The Structure of Biological Membranes , pp. 201-241
    • Rand, R.P.1    Parsegian, V.A.2
  • 110
    • 65249084081 scopus 로고    scopus 로고
    • A phenomenological one-parameter equation of state for osmotic pressures of PEG and other neutral flexible polymers in good solvents
    • J.A. Cohen, R. Podgornik, P.L. Hansen, and V.A. Parsegian A phenomenological one-parameter equation of state for osmotic pressures of PEG and other neutral flexible polymers in good solvents J. Phys. Chem. B 113 2009 3709 3714
    • (2009) J. Phys. Chem. B , vol.113 , pp. 3709-3714
    • Cohen, J.A.1    Podgornik, R.2    Hansen, P.L.3    Parsegian, V.A.4
  • 111
    • 0029157334 scopus 로고
    • Temperature dependence of the repulsive pressure between phosphatidylcholine bilayers
    • S.A. Simon, S. Advanti, and T.J. McIntosh Temperature dependence of the repulsive pressure between phosphatidylcholine bilayers Biophys. J. 69 1995 1473 1483
    • (1995) Biophys. J. , vol.69 , pp. 1473-1483
    • Simon, S.A.1    Advanti, S.2    McIntosh, T.J.3
  • 112
    • 0022459444 scopus 로고
    • Osmotic stress for the direct measurement of intermolecular forces
    • V.A. Parsegian, R.P. Rand, N.L. Fuller, and D.C. Rau Osmotic stress for the direct measurement of intermolecular forces Methods Enzymol. 127 1986 400 416
    • (1986) Methods Enzymol. , vol.127 , pp. 400-416
    • Parsegian, V.A.1    Rand, R.P.2    Fuller, N.L.3    Rau, D.C.4
  • 113
    • 0029130871 scopus 로고
    • Macromolecules and water: Probing with osmotic stress
    • V.A. Parsegian, R.P. Rand, and D.C. Rau Macromolecules and water: probing with osmotic stress Methods Enzymol. 259 1995 43 94
    • (1995) Methods Enzymol. , vol.259 , pp. 43-94
    • Parsegian, V.A.1    Rand, R.P.2    Rau, D.C.3
  • 115
    • 0019363272 scopus 로고
    • Interacting phospholipid bilayers: Measured forces and induced structural changes
    • R.P. Rand Interacting phospholipid bilayers: measured forces and induced structural changes Annu. Rev. Biophys. Bioeng. 10 1981 277 314
    • (1981) Annu. Rev. Biophys. Bioeng. , vol.10 , pp. 277-314
    • Rand, R.P.1
  • 118
    • 0031022195 scopus 로고    scopus 로고
    • On a possible microscopic mechanism underlying the vapor pressure paradox
    • R. Podgornik, and V.A. Parsegian On a possible microscopic mechanism underlying the vapor pressure paradox Biophys. J. 72 1997 942 952
    • (1997) Biophys. J. , vol.72 , pp. 942-952
    • Podgornik, R.1    Parsegian, V.A.2
  • 119
    • 0033151158 scopus 로고    scopus 로고
    • Absence of a vestigial vapor pressure paradox
    • J.F. Nagle, and J. Katsaras Absence of a vestigial vapor pressure paradox Phys. Rev. E. 59 1999 7018 7024
    • (1999) Phys. Rev. E. , vol.59 , pp. 7018-7024
    • Nagle, J.F.1    Katsaras, J.2
  • 120
    • 0031910473 scopus 로고    scopus 로고
    • Effect of substrate roughness on D spacing supports theoretical resolution of vapor pressure paradox
    • S. Tristram-Nagle, H.I. Petrache, R.M. Suter, and J.F. Nagle Effect of substrate roughness on D spacing supports theoretical resolution of vapor pressure paradox Biophys. J. 74 1998 1421 1427
    • (1998) Biophys. J. , vol.74 , pp. 1421-1427
    • Tristram-Nagle, S.1    Petrache, H.I.2    Suter, R.M.3    Nagle, J.F.4
  • 122
    • 0024280716 scopus 로고
    • Structure of fully hydrated bilayer dispersions
    • J.F. Nagle, and M.C. Wiener Structure of fully hydrated bilayer dispersions Biochim. Biophys. Acta 942 1988 1 10
    • (1988) Biochim. Biophys. Acta , vol.942 , pp. 1-10
    • Nagle, J.F.1    Wiener, M.C.2
  • 123
    • 0001477831 scopus 로고
    • Interphases of chain molecules: Monolayers and lipid bilayer membranes
    • K.A. Dill, and P.J. Flory Interphases of chain molecules: monolayers and lipid bilayer membranes Proc. Natl. Acad. Sci. U. S. A. 77 1980 3115 3119
    • (1980) Proc. Natl. Acad. Sci. U. S. A. , vol.77 , pp. 3115-3119
    • Dill, K.A.1    Flory, P.J.2
  • 125
    • 85051913010 scopus 로고    scopus 로고
    • Effect of chain unsaturation on bilayer response to pressure
    • 051913-1-051913-8
    • I.D. Skanes, J. Steward, K.M.W. Keough, and M.R. Morrow Effect of chain unsaturation on bilayer response to pressure Phys. Rev. E. 74 2006 051913-1-051913-8
    • (2006) Phys. Rev. E. , vol.74
    • Skanes, I.D.1    Steward, J.2    Keough, K.M.W.3    Morrow, M.R.4
  • 126
    • 0023043180 scopus 로고
    • Hydrostatic pressure induces hydrocarbon chain interdigitation in single-component phospholipid bilayers
    • L.F. Braganza, and D.L. Worcester Hydrostatic pressure induces hydrocarbon chain interdigitation in single-component phospholipid bilayers Biochemistry 25 1986 2591 2596
    • (1986) Biochemistry , vol.25 , pp. 2591-2596
    • Braganza, L.F.1    Worcester, D.L.2
  • 127
    • 84877040209 scopus 로고    scopus 로고
    • Introductory lecture: Basic quantities in model biomembranes
    • J.F. Nagle Introductory lecture: basic quantities in model biomembranes Faraday Discuss. 161 2013 11 29
    • (2013) Faraday Discuss. , vol.161 , pp. 11-29
    • Nagle, J.F.1
  • 128
    • 0037125502 scopus 로고    scopus 로고
    • Elastic deformation of membrane bilayers probed by deuterium NMR relaxation
    • M.F. Brown, R.L. Thurmond, S.W. Dodd, D. Otten, and K. Beyer Elastic deformation of membrane bilayers probed by deuterium NMR relaxation J. Am. Chem. Soc. 124 2002 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
  • 129
  • 130
    • 78951491640 scopus 로고    scopus 로고
    • An NMR database for simulations of membrane dynamics
    • A. Leftin, and M.F. Brown An NMR database for simulations of membrane dynamics Biochim. Biophys. Acta 1808 2011 818 839
    • (2011) Biochim. Biophys. Acta , vol.1808 , pp. 818-839
    • Leftin, A.1    Brown, M.F.2
  • 131
    • 78651253456 scopus 로고    scopus 로고
    • Protein diffusion in the periplasm of E coli under osmotic stress
    • K.A. Sochacki, I.A. Shkel, M.T. Record, and J.C. Weisshaar Protein diffusion in the periplasm of E. coli under osmotic stress Biophys. J. 100 2011 22 31
    • (2011) Biophys. J. , vol.100 , pp. 22-31
    • Sochacki, K.A.1    Shkel, I.A.2    Record, M.T.3    Weisshaar, J.C.4
  • 132
    • 76749110236 scopus 로고    scopus 로고
    • Osmolytes modulate conformational exchange in solvent-exposed regions of membrane proteins
    • R.H.F. Jiménez, M.-A. Do Cao, M. Kim, and D.S. Cafiso Osmolytes modulate conformational exchange in solvent-exposed regions of membrane proteins Protein Sci. 19 2010 269 278
    • (2010) Protein Sci. , vol.19 , pp. 269-278
    • Jiménez, R.H.F.1    Do Cao, M.-A.2    Kim, M.3    Cafiso, D.S.4
  • 133
    • 0017260691 scopus 로고
    • Apparent modification of forces between lecithin bilayers
    • D.M. LeNeveu, R.P. Rand, D. Gingell, and V.A. Parsegian Apparent modification of forces between lecithin bilayers Science 191 1976 399 400
    • (1976) Science , vol.191 , pp. 399-400
    • Leneveu, D.M.1    Rand, R.P.2    Gingell, D.3    Parsegian, V.A.4
  • 134
    • 33846451059 scopus 로고    scopus 로고
    • Self-induced docking site of a deeply embedded peripheral membrane protein
    • S. Jaud, D.J. Tobias, J.J. Falke, and S.H. White Self-induced docking site of a deeply embedded peripheral membrane protein Biophys. J. 92 2007 517 524
    • (2007) Biophys. J. , vol.92 , pp. 517-524
    • Jaud, S.1    Tobias, D.J.2    Falke, J.J.3    White, S.H.4
  • 136
    • 77956683194 scopus 로고    scopus 로고
    • Influence of non-lamellar forming lipids on rhodopsin
    • M.F. Brown Influence of non-lamellar forming lipids on rhodopsin Curr. Top. Membr. 44 1997 285 356
    • (1997) Curr. Top. Membr. , vol.44 , pp. 285-356
    • Brown, M.F.1
  • 137
    • 0037194760 scopus 로고    scopus 로고
    • Open channel structure of Mscl and the gating mechanism of mechanosensitive channels
    • E. Perozo, D.M. Cortes, P. Sompornpisut, A. Kloda, and B. Martinac Open channel structure of Mscl and the gating mechanism of mechanosensitive channels Nature 418 2002 942 948
    • (2002) Nature , vol.418 , pp. 942-948
    • Perozo, E.1    Cortes, D.M.2    Sompornpisut, P.3    Kloda, A.4    Martinac, B.5
  • 138
    • 84855416611 scopus 로고    scopus 로고
    • Direct measurement of the mechanical properties of lipid phases in supported bilayers
    • L. Picas, F. Rico, and S. Scheuring Direct measurement of the mechanical properties of lipid phases in supported bilayers Biophys. J. 102 2012 L1 L3
    • (2012) Biophys. J. , vol.102 , pp. 1-L3
    • Picas, L.1    Rico, F.2    Scheuring, S.3
  • 139
    • 79953740665 scopus 로고    scopus 로고
    • Thermodynamics and mechanics of membrane curvature generation and sensing by proteins and lipids
    • T. Baumgart, B.R. Capraro, C. Zhu, and S.L. Das Thermodynamics and mechanics of membrane curvature generation and sensing by proteins and lipids Annu. Rev. Phys. Chem. 62 2011 483 506
    • (2011) Annu. Rev. Phys. Chem. , vol.62 , pp. 483-506
    • Baumgart, T.1    Capraro, B.R.2    Zhu, C.3    Das, S.L.4
  • 140
    • 79959928058 scopus 로고    scopus 로고
    • Side-chain hydrophobicity scale derived from transmembrane protein folding into lipid bilayers
    • C.P. Moon, and K.G. Fleming Side-chain hydrophobicity scale derived from transmembrane protein folding into lipid bilayers Proc. Natl. Acad. Sci. U. S. A. 108 2011 10174 10177
    • (2011) Proc. Natl. Acad. Sci. U. S. A. , vol.108 , pp. 10174-10177
    • Moon, C.P.1    Fleming, K.G.2


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