메뉴 건너뛰기




Volumn 90, Issue 6, 2006, Pages 1855-1864

Conformation and environment of channel-forming peptides: A simulation study

Author keywords

[No Author keywords available]

Indexed keywords

DETERGENT; GLYCINE RECEPTOR; HYDROGEN; LIPID; PEPTIDE; TRIFLUOROETHANOL; WATER;

EID: 33646005837     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1529/biophysj.105.069625     Document Type: Article
Times cited : (18)

References (85)
  • 1
    • 0031954925 scopus 로고    scopus 로고
    • Genome-wide analysis of integral membrane proteins from eubacterial, archean, and eukaryotic organisms
    • Wallin, E., and G. von Heijne. 1998. Genome-wide analysis of integral membrane proteins from eubacterial, archean, and eukaryotic organisms. Protein Sci. 7:1029-1038.
    • (1998) Protein Sci. , vol.7 , pp. 1029-1038
    • Wallin, E.1    Von Heijne, G.2
  • 3
    • 3042621274 scopus 로고    scopus 로고
    • The progress of membrane protein structure determination
    • White, S. H. 2004. The progress of membrane protein structure determination. Protein Sci. 13:1948-1949.
    • (2004) Protein Sci. , vol.13 , pp. 1948-1949
    • White, S.H.1
  • 4
    • 0033790343 scopus 로고    scopus 로고
    • Helical membrane protein folding, stability, and evolution
    • Popot, J. L., and D. M. Engelman. 2000. Helical membrane protein folding, stability, and evolution. Annu. Rev. Biochem. 69:881-922.
    • (2000) Annu. Rev. Biochem. , vol.69 , pp. 881-922
    • Popot, J.L.1    Engelman, D.M.2
  • 5
    • 0033982348 scopus 로고    scopus 로고
    • Solution structure of the sixth transmembrane helix of the G-protein-coupled receptor, rhodopsin
    • Chopra, A., P. L. Yeagle, J. A. Alderfer, and A. D. Albert. 2000. Solution structure of the sixth transmembrane helix of the G-protein-coupled receptor, rhodopsin. Biochim. Biophys. Acta. 1463:1-5.
    • (2000) Biochim. Biophys. Acta , vol.1463 , pp. 1-5
    • Chopra, A.1    Yeagle, P.L.2    Alderfer, J.A.3    Albert, A.D.4
  • 6
    • 0030932407 scopus 로고    scopus 로고
    • A transmembrane helix dimer: Structure and implications
    • MacKenzie, K. R., J. H. Prestegard, and D. M. Engelman. 1997. A transmembrane helix dimer: structure and implications. Science. 276:131-133.
    • (1997) Science , vol.276 , pp. 131-133
    • MacKenzie, K.R.1    Prestegard, J.H.2    Engelman, D.M.3
  • 7
    • 0035811042 scopus 로고    scopus 로고
    • Structure of the transmembrane dimer interface of glycophorin A in membrane bilayers
    • Smith, S. O., D. Song, S. Shekar, M. Groesbeek, M. Ziliox, and S. Aimoto. 2001. Structure of the transmembrane dimer interface of glycophorin A in membrane bilayers. Biochemistry. 40:6553-6558.
    • (2001) Biochemistry , vol.40 , pp. 6553-6558
    • Smith, S.O.1    Song, D.2    Shekar, S.3    Groesbeek, M.4    Ziliox, M.5    Aimoto, S.6
  • 8
    • 0025249842 scopus 로고
    • Membrane protein folding and oligomerization: The two-state model
    • Popot, J. L., and D. M. Engelman. 1990. Membrane protein folding and oligomerization: the two-state model. Biochemistry. 29:4031-4037.
    • (1990) Biochemistry , vol.29 , pp. 4031-4037
    • Popot, J.L.1    Engelman, D.M.2
  • 10
    • 0027264459 scopus 로고
    • Integral membrane protein structure: Transmembrane α helices as autonomous folding domains
    • Popot, J. L. 1993. Integral membrane protein structure: transmembrane α helices as autonomous folding domains. Curr. Opin. Struct. Biol. 3:532-540.
    • (1993) Curr. Opin. Struct. Biol. , vol.3 , pp. 532-540
    • Popot, J.L.1
  • 11
    • 0033983453 scopus 로고    scopus 로고
    • Asparagine-mediated self-association of a model transmembrane helix
    • Choma, C., H. Gratkowski, J. D. Lear, and W. F. DeGrado. 2000. Asparagine-mediated self-association of a model transmembrane helix. Nat. Struct. Biol. 7:161-166.
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 161-166
    • Choma, C.1    Gratkowski, H.2    Lear, J.D.3    DeGrado, W.F.4
  • 13
    • 0025935264 scopus 로고
    • The biophysics of peptide models of ion channels
    • Sansom, M. S. P. 1991. The biophysics of peptide models of ion channels. Prog. Biophys. Mol. Biol. 55:139-236.
    • (1991) Prog. Biophys. Mol. Biol. , vol.55 , pp. 139-236
    • Sansom, M.S.P.1
  • 14
    • 0027817476 scopus 로고
    • Structure and function of channel-forming peptaibols
    • Sansom, M. S. P. 1993. Structure and function of channel-forming peptaibols. Q. Rev. Biophys. 26:365-421.
    • (1993) Q. Rev. Biophys. , vol.26 , pp. 365-421
    • Sansom, M.S.P.1
  • 15
    • 0030602182 scopus 로고    scopus 로고
    • Identification of an ion channel activity of the Vpu transmembrane domain and its involvement in the regulation of virus release from HIV-1-infected cells
    • Schubert, U., A. V. Ferrer-Montiel, M. Oblatt-Montal, P. Henklein, K. Strebel, and M. Montal. 1996. Identification of an ion channel activity of the Vpu transmembrane domain and its involvement in the regulation of virus release from HIV-1-infected cells. FEBS Lett. 398:12-18.
    • (1996) FEBS Lett. , vol.398 , pp. 12-18
    • Schubert, U.1    Ferrer-Montiel, A.V.2    Oblatt-Montal, M.3    Henklein, P.4    Strebel, K.5    Montal, M.6
  • 16
    • 0023907575 scopus 로고
    • Synthetic amphiphilic peptide models for protein ion channels
    • Lear, J. D., Z. R. Wasserman, and W. F. DeGrado. 1988. Synthetic amphiphilic peptide models for protein ion channels. Science. 240:1177-1181.
    • (1988) Science , vol.240 , pp. 1177-1181
    • Lear, J.D.1    Wasserman, Z.R.2    DeGrado, W.F.3
  • 17
    • 0010528163 scopus 로고
    • M2δ, a candidate for the structure lining the ionic channel of the nicotinic cholinergic receptor
    • Oiki, S., W. Danho, V. Madison, and M. Montal. 1988. M2δ, a candidate for the structure lining the ionic channel of the nicotinic cholinergic receptor. Proc. Natl. Acad. Sci. USA. 85:8703-8707.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 8703-8707
    • Oiki, S.1    Danho, W.2    Madison, V.3    Montal, M.4
  • 18
    • 0029150299 scopus 로고
    • Design of molecular function: Channels of communication
    • Montal, M. 1995. Design of molecular function: channels of communication. Annu. Rev. Biophys. Biomol. Struct. 24:31-57.
    • (1995) Annu. Rev. Biophys. Biomol. Struct. , vol.24 , pp. 31-57
    • Montal, M.1
  • 19
    • 0032919444 scopus 로고    scopus 로고
    • Structures of the M2 channel-lining segments from nicotinic acetylcholine and NMDA receptors by NMR spectroscopy
    • Opella, S. J., F. M. Marassi, J. J. Gesell, A. P. Valente, Y. Kim, M. Oblatt-Montal, and M. Montal. 1999. Structures of the M2 channel-lining segments from nicotinic acetylcholine and NMDA receptors by NMR spectroscopy. Nat. Struct. Biol. 6:374-379.
    • (1999) Nat. Struct. Biol. , vol.6 , pp. 374-379
    • Opella, S.J.1    Marassi, F.M.2    Gesell, J.J.3    Valente, A.P.4    Kim, Y.5    Oblatt-Montal, M.6    Montal, M.7
  • 20
    • 0033996292 scopus 로고    scopus 로고
    • Structure and dynamics of the pore-lining helix of the nicotinic receptor: MD simulations in water, lipid bilayers and transbilayer bundles
    • Law, R. J., L. R. Forrest, K. M. Ranatunga, P. La Rocca, D. P. Tieleman, and M. S. P. Sansom. 2000. Structure and dynamics of the pore-lining helix of the nicotinic receptor: MD simulations in water, lipid bilayers and transbilayer bundles. Proteins. 39:47-55.
    • (2000) Proteins , vol.39 , pp. 47-55
    • Law, R.J.1    Forrest, L.R.2    Ranatunga, K.M.3    La Rocca, P.4    Tieleman, D.P.5    Sansom, M.S.P.6
  • 21
    • 12244294449 scopus 로고    scopus 로고
    • Pores formed by the nicotinic receptor M2δ peptide: A molecular dynamics simulation study
    • Law, R. J., D. P. Tieleman, and M. S. P. Sansom. 2003. Pores formed by the nicotinic receptor M2δ peptide: a molecular dynamics simulation study. Biophys. J. 84:14-27.
    • (2003) Biophys. J. , vol.84 , pp. 14-27
    • Law, R.J.1    Tieleman, D.P.2    Sansom, M.S.P.3
  • 23
    • 20544431791 scopus 로고    scopus 로고
    • Structure and dynamics of the second and third transmembrane domain of human glycine receptor
    • Ma, D., Z. Liu, L. Li, P. Tang, and Y. Xu. 2005. Structure and dynamics of the second and third transmembrane domain of human glycine receptor. Biochemistry. 44:8790-8800.
    • (2005) Biochemistry , vol.44 , pp. 8790-8800
    • Ma, D.1    Liu, Z.2    Li, L.3    Tang, P.4    Xu, Y.5
  • 24
    • 13444271681 scopus 로고    scopus 로고
    • Refined structure of the nicotinic acetylcholine receptor at 4 Å resolution
    • Unwin, N. 2005. Refined structure of the nicotinic acetylcholine receptor at 4 Å resolution. J. Mol. Biol. 346:967-989.
    • (2005) J. Mol. Biol. , vol.346 , pp. 967-989
    • Unwin, N.1
  • 25
    • 0027255102 scopus 로고
    • Synthetic peptides and four-helix bundle proteins as model systems for the pore-forming structure of channel proteins. II. Transmembrane segment M2 of the brain glycine receptor is a plausible candidate for the pore-lining structure
    • Reddy, G. L., T. Iwamoto, J. M. Tomich, and M. Montal. 1993. Synthetic peptides and four-helix bundle proteins as model systems for the pore-forming structure of channel proteins. II. Transmembrane segment M2 of the brain glycine receptor is a plausible candidate for the pore-lining structure. J. Biol. Chem. 268:14608-14615.
    • (1993) J. Biol. Chem. , vol.268 , pp. 14608-14615
    • Reddy, G.L.1    Iwamoto, T.2    Tomich, J.M.3    Montal, M.4
  • 26
    • 10744223669 scopus 로고    scopus 로고
    • Activity and structural comparisons of solution associating and monomeric channel-forming peptides derived from the glycine receptor M2 segment
    • Cook, G. A., O. Prakash, K. Zhang, L. P. Shank, W. A. Takeguchi, A. Robbins, Y. X. Gong, T. Iwamoto, B. D. Schultz, and J. M. Tomich. 2004. Activity and structural comparisons of solution associating and monomeric channel-forming peptides derived from the glycine receptor M2 segment. Biophys. J. 86:1424-1435.
    • (2004) Biophys. J. , vol.86 , pp. 1424-1435
    • Cook, G.A.1    Prakash, O.2    Zhang, K.3    Shank, L.P.4    Takeguchi, W.A.5    Robbins, A.6    Gong, Y.X.7    Iwamoto, T.8    Schultz, B.D.9    Tomich, J.M.10
  • 28
    • 0034703270 scopus 로고    scopus 로고
    • Modulation of glycophorin A transmembrane helix interactions by lipid bilayers: Molecular dynamics calculations
    • Petrache, H. I., A. Grossfield, K. R. MacKenzie, D. M. Engelman, and T. B. Woolf. 2000. Modulation of glycophorin A transmembrane helix interactions by lipid bilayers: molecular dynamics calculations. J. Mol. Biol. 302:727-746.
    • (2000) J. Mol. Biol. , vol.302 , pp. 727-746
    • Petrache, H.I.1    Grossfield, A.2    MacKenzie, K.R.3    Engelman, D.M.4    Woolf, T.B.5
  • 30
    • 13944255096 scopus 로고    scopus 로고
    • Understanding the energetics of helical peptide orientation in membranes
    • Sengupta, D., L. Meinhold, D. Langosch, G. M. Ullmann, and J. C. Smith. 2005. Understanding the energetics of helical peptide orientation in membranes. Proteins. 58:913-922.
    • (2005) Proteins , vol.58 , pp. 913-922
    • Sengupta, D.1    Meinhold, L.2    Langosch, D.3    Ullmann, G.M.4    Smith, J.C.5
  • 31
    • 0038724257 scopus 로고    scopus 로고
    • Membrane protein dynamics vs. environment: Simulations of OmpA in a micelle and in a bilayer
    • Bond, P. J., and M. S. P. Sansom. 2003. Membrane protein dynamics vs. environment: simulations of OmpA in a micelle and in a bilayer. J. Mol. Biol. 329:1035-1053.
    • (2003) J. Mol. Biol. , vol.329 , pp. 1035-1053
    • Bond, P.J.1    Sansom, M.S.P.2
  • 32
    • 10344247720 scopus 로고    scopus 로고
    • MD simulations of spontaneous membrane protein/detergent micelle formation
    • Bond, P. J., J. M. Cuthbertson, S. D. Deol, and M. S. P. Sansom. 2004. MD simulations of spontaneous membrane protein/detergent micelle formation. J. Am. Chem. Soc. 126:15948-15949.
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 15948-15949
    • Bond, P.J.1    Cuthbertson, J.M.2    Deol, S.D.3    Sansom, M.S.P.4
  • 33
    • 4143150532 scopus 로고    scopus 로고
    • Molecular dynamics simulations of micelle formation around dimeric glycophorin A transmembrane helices
    • Braun, R., D. M. Engelman, and K. Schulten. 2004. Molecular dynamics simulations of micelle formation around dimeric glycophorin A transmembrane helices. Biophys. J. 87:754-763.
    • (2004) Biophys. J. , vol.87 , pp. 754-763
    • Braun, R.1    Engelman, D.M.2    Schulten, K.3
  • 34
    • 12244294104 scopus 로고    scopus 로고
    • Structure of the pore region of the nicotinic acetylcholine receptor ion channel: A molecular dynamics simulation study
    • Abstr..
    • Saiz, L., and M. L. Klein. 2002. Structure of the pore region of the nicotinic acetylcholine receptor ion channel: a molecular dynamics simulation study. Biophys. J. 82:560a. (Abstr.).
    • (2002) Biophys. J. , vol.82
    • Saiz, L.1    Klein, M.L.2
  • 35
    • 1542365497 scopus 로고    scopus 로고
    • Effect of the pore region of a transmembrane ion channel on the physical properties of a simple membrane
    • Saiz, L., S. Bandyopadhyay, and M. L. Klein. 2004. Effect of the pore region of a transmembrane ion channel on the physical properties of a simple membrane. J. Phys. Chem. B. 108:2608-2613.
    • (2004) J. Phys. Chem. B. , vol.108 , pp. 2608-2613
    • Saiz, L.1    Bandyopadhyay, S.2    Klein, M.L.3
  • 36
    • 0344551149 scopus 로고    scopus 로고
    • Interactions of hydrophobic peptides with lipid bilayers: Monte Carlo simulations with M2 delta
    • Kessel, A., D. Shental-Bechor, T. Haliloglu, and N. Ben-Tal. 2003. Interactions of hydrophobic peptides with lipid bilayers: Monte Carlo simulations with M2 delta. Biophys. J. 85:3431-3444.
    • (2003) Biophys. J. , vol.85 , pp. 3431-3444
    • Kessel, A.1    Shental-Bechor, D.2    Haliloglu, T.3    Ben-Tal, N.4
  • 37
    • 0037126023 scopus 로고    scopus 로고
    • Mechanism by which 2,2,2-trifluoroethanol/water mixtures stabilize secondary-structure formation in peptides: A molecular dynamics study
    • Roccatano, D., G. Colombo, M. Fioroni, and A. E. Mark. 2002. Mechanism by which 2,2,2-trifluoroethanol/water mixtures stabilize secondary-structure formation in peptides: a molecular dynamics study. Proc. Natl. Acad. Sci. USA. 99:12179-12184.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 12179-12184
    • Roccatano, D.1    Colombo, G.2    Fioroni, M.3    Mark, A.E.4
  • 38
    • 0037027953 scopus 로고    scopus 로고
    • Peptide conformational changes induced by tryptophan-phosphocholine interactions in a micelle
    • Neidigh, J. W., and N. H. Andersen. 2002. Peptide conformational changes induced by tryptophan-phosphocholine interactions in a micelle. Biopolymers. 65:354-361.
    • (2002) Biopolymers , vol.65 , pp. 354-361
    • Neidigh, J.W.1    Andersen, N.H.2
  • 39
    • 0036286167 scopus 로고    scopus 로고
    • NMR structures of the second transmembrane domain of the human glycine receptor alpha(1) subunit: Model of pore architecture and channel gating
    • Tang, P., P. K. Mandal, and Y. Xu. 2002. NMR structures of the second transmembrane domain of the human glycine receptor alpha(1) subunit: model of pore architecture and channel gating. Biophys. J. 83:252-262.
    • (2002) Biophys. J. , vol.83 , pp. 252-262
    • Tang, P.1    Mandal, P.K.2    Xu, Y.3
  • 40
    • 0037062632 scopus 로고    scopus 로고
    • Distinct structural elements that direct solution aggregation and membrane assembly in the channel forming peptide M2GlyR
    • Broughman, J. R., L. P. Shank, W. Takeguchi, T. Iwamoto, K. E. Mitchell, B. D. Schultz, and J. M. Tomich. 2002. Distinct structural elements that direct solution aggregation and membrane assembly in the channel forming peptide M2GlyR. Biochemistry. 41:7350-7358.
    • (2002) Biochemistry , vol.41 , pp. 7350-7358
    • Broughman, J.R.1    Shank, L.P.2    Takeguchi, W.3    Iwamoto, T.4    Mitchell, K.E.5    Schultz, B.D.6    Tomich, J.M.7
  • 41
    • 0028070549 scopus 로고
    • Parallel helix bundles and ion channels: Molecular modelling via simulated annealing and restrained molecular dynamics
    • Kerr, I. D., R. Sankararamakrishnan, O. S. Smart, and M. S. P. Sansom. 1994. Parallel helix bundles and ion channels: molecular modelling via simulated annealing and restrained molecular dynamics. Biophys. J. 67:1501-1515.
    • (1994) Biophys. J. , vol.67 , pp. 1501-1515
    • Kerr, I.D.1    Sankararamakrishnan, R.2    Smart, O.S.3    Sansom, M.S.P.4
  • 42
    • 0027518118 scopus 로고
    • Hydrophilic surface maps of α-helical channel-forming peptides
    • Kerr, I. D., and M. S. P. Sansom. 1993. Hydrophilic surface maps of α-helical channel-forming peptides. Eur. Biophys. J. 22:269-277.
    • (1993) Eur. Biophys. J. , vol.22 , pp. 269-277
    • Kerr, I.D.1    Sansom, M.S.P.2
  • 43
    • 0035789518 scopus 로고    scopus 로고
    • GROMACS 3.0: A package for molecular simulation and trajectory analysis
    • Lindahl, E., B. Hess, and D. van der Spoel. 2001. GROMACS 3.0: a package for molecular simulation and trajectory analysis. J. Mol. Model. [Online]. 7:306-317.
    • (2001) J. Mol. Model. [Online] , vol.7 , pp. 306-317
    • Lindahl, E.1    Hess, B.2    Van Der Spoel, D.3
  • 45
    • 0343614206 scopus 로고    scopus 로고
    • A systematic study of water models for molecular simulations
    • van der Spoel, D., P. J. van Maaren, and H. J. C. Berendsen. 1998. A systematic study of water models for molecular simulations. J. Chem. Phys. 108:10220-10230.
    • (1998) J. Chem. Phys. , vol.108 , pp. 10220-10230
    • Van Der Spoel, D.1    Van Maaren, P.J.2    Berendsen, H.J.C.3
  • 47
    • 84943502952 scopus 로고
    • A molecular dynamics method for simulations in the canonical ensemble
    • Nose, S. 1984. A molecular dynamics method for simulations in the canonical ensemble. Mol. Phys. 52:255-268.
    • (1984) Mol. Phys. , vol.52 , pp. 255-268
    • Nose, S.1
  • 48
    • 0001538909 scopus 로고
    • Canonical dynamics: Equilibrium phase-space distributions
    • Hoover, W. G. 1985. Canonical dynamics: equilibrium phase-space distributions. Phys. Rev. A31:1695-1697.
    • (1985) Phys. Rev. , vol.A31 , pp. 1695-1697
    • Hoover, W.G.1
  • 49
    • 0019707626 scopus 로고
    • Polymorphic transitions in single-crystals: A new molecular-dynamics method
    • Parrinello, M., and A. Rahman. 1981. Polymorphic transitions in single-crystals: a new molecular-dynamics method. J. Appl. Phys. 52:7182-7190.
    • (1981) J. Appl. Phys. , vol.52 , pp. 7182-7190
    • Parrinello, M.1    Rahman, A.2
  • 50
    • 33846823909 scopus 로고
    • Particle mesh Ewald: An N.log(N) method for Ewald sums in large systems
    • Darden, T., D. York, and L. Pedersen. 1993. Particle mesh Ewald: an N.log(N) method for Ewald sums in large systems. J. Chem. Phys. 98:10089-10092.
    • (1993) J. Chem. Phys. , vol.98 , pp. 10089-10092
    • Darden, T.1    York, D.2    Pedersen, L.3
  • 52
    • 0034499271 scopus 로고    scopus 로고
    • A new 2,2,2-trifluoroethanol model for molecular dynamics simulations
    • Fioroni, M., K. Burger, A. E. Mark, and D. Roccatano. 2000. A new 2,2,2-trifluoroethanol model for molecular dynamics simulations. J. Phys. Chem. B. 104:12347-12354.
    • (2000) J. Phys. Chem. B. , vol.104 , pp. 12347-12354
    • Fioroni, M.1    Burger, K.2    Mark, A.E.3    Roccatano, D.4
  • 53
    • 0037014684 scopus 로고    scopus 로고
    • Solvation phenomena of a tetrapeptide in water/trifluoroethanol and water/ethanol mixtures: A diffusion NMR, intermolecular NOE, and molecular dynamics study
    • Fioroni, M., M. D. Diaz, K. Burger, and S. Berger. 2002. Solvation phenomena of a tetrapeptide in water/trifluoroethanol and water/ethanol mixtures: a diffusion NMR, intermolecular NOE, and molecular dynamics study. J. Am. Chem. Soc. 124:7737-7744.
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 7737-7744
    • Fioroni, M.1    Diaz, M.D.2    Burger, K.3    Berger, S.4
  • 54
    • 0030158429 scopus 로고    scopus 로고
    • PRODRG, a program for generating molecular topologies and unique molecular descriptors from coordinates of small molecules
    • van Aalten, D. M., R. Bywater, J. B. Findlay, M. Hendlich, R. W. Hooft, and G. Vriend. 1996. PRODRG, a program for generating molecular topologies and unique molecular descriptors from coordinates of small molecules. J. Comput. Aided Mol. Des. 10:255-262.
    • (1996) J. Comput. Aided Mol. Des. , vol.10 , pp. 255-262
    • Van Aalten, D.M.1    Bywater, R.2    Findlay, J.B.3    Hendlich, M.4    Hooft, R.W.5    Vriend, G.6
  • 55
  • 56
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: Pattern-recognition of hydrogen-bonded and geometrical features
    • Kabsch, W., and C. Sander. 1983. Dictionary of protein secondary structure: pattern-recognition of hydrogen-bonded and geometrical features. Biopolymers. 22:2577-2637.
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 57
    • 0000243829 scopus 로고
    • Procheck: A program to check the stereochemical quality of protein structures
    • Laskowski, R. A., M. W. Macarthur, D. S. Moss, and J. M. Thornton. 1993. Procheck: a program to check the stereochemical quality of protein structures. J. Appl. Crystallogr. 26:283-291.
    • (1993) J. Appl. Crystallogr. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    Macarthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 60
    • 0026557830 scopus 로고
    • The functions of tryptophan residues in membrane proteins
    • Schiffer, M., C. H. Chang, and F. J. Stevens. 1992. The functions of tryptophan residues in membrane proteins. Protein Eng. 5:213-214.
    • (1992) Protein Eng. , vol.5 , pp. 213-214
    • Schiffer, M.1    Chang, C.H.2    Stevens, F.J.3
  • 61
    • 0032552880 scopus 로고    scopus 로고
    • The preference of tryptophan for membrane interfaces
    • Yau, W. M., W. C. Wimley, K. Gawrisch, and S. H. White. 1998. The preference of tryptophan for membrane interfaces. Biochemistry. 37:14713-14718.
    • (1998) Biochemistry , vol.37 , pp. 14713-14718
    • Yau, W.M.1    Wimley, W.C.2    Gawrisch, K.3    White, S.H.4
  • 62
    • 0037881905 scopus 로고    scopus 로고
    • Interfacial anchor properties of tryptophan residues in transmembrane peptides can dominate over hydrophobic matching effects in peptide-lipid interactions
    • de Planque, M. R., B. B. Bonev, J. A. Demmers, D. V. Greathouse, R. E. Koeppe, F. Separovic, A. Watts, and J. A. Killian. 2003. Interfacial anchor properties of tryptophan residues in transmembrane peptides can dominate over hydrophobic matching effects in peptide-lipid interactions. Biochemistry. 42:5341-5348.
    • (2003) Biochemistry , vol.42 , pp. 5341-5348
    • De Planque, M.R.1    Bonev, B.B.2    Demmers, J.A.3    Greathouse, D.V.4    Koeppe, R.E.5    Separovic, F.6    Watts, A.7    Killian, J.A.8
  • 63
    • 10044244661 scopus 로고    scopus 로고
    • Lipid-protein interactions of integral membrane proteins: A comparative simulation study
    • Deol, S. S., P. J. Bond, C. Domene, and M. S. P. Sansom. 2004. Lipid-protein interactions of integral membrane proteins: a comparative simulation study. Biophys. J. 87:3737-3749.
    • (2004) Biophys. J. , vol.87 , pp. 3737-3749
    • Deol, S.S.1    Bond, P.J.2    Domene, C.3    Sansom, M.S.P.4
  • 64
    • 0022804939 scopus 로고
    • Stabilization of the ribonuclease S-peptide alpha-helix by trifluoroethanol
    • Nelson, J. W., and N. R. Kallenbach. 1986. Stabilization of the ribonuclease S-peptide alpha-helix by trifluoroethanol. Proteins. 1:211-217.
    • (1986) Proteins , vol.1 , pp. 211-217
    • Nelson, J.W.1    Kallenbach, N.R.2
  • 65
    • 0028978422 scopus 로고
    • Trifluoroethanol-induced stabilization of the alpha-helical structure of beta-lactoglobulin: Implication for non-hierarchical protein folding
    • Shiraki, K., K. Nishikawa, and Y. Goto. 1995. Trifluoroethanol-induced stabilization of the alpha-helical structure of beta-lactoglobulin: implication for non-hierarchical protein folding. J. Mol. Biol. 245:180-194.
    • (1995) J. Mol. Biol. , vol.245 , pp. 180-194
    • Shiraki, K.1    Nishikawa, K.2    Goto, Y.3
  • 66
    • 0033595582 scopus 로고    scopus 로고
    • Clustering of fluorine-substituted alcohols as a factor responsible for their marked effects on proteins and peptides
    • Hong, D. P., M. Hoshino, R. Kuboi, and Y. Goto. 1999. Clustering of fluorine-substituted alcohols as a factor responsible for their marked effects on proteins and peptides. J. Am. Chem. Soc. 121:8427-8433.
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 8427-8433
    • Hong, D.P.1    Hoshino, M.2    Kuboi, R.3    Goto, Y.4
  • 67
    • 0035795721 scopus 로고    scopus 로고
    • Amino acid distributions in integral membrane protein structures
    • Ulmschneider, M. B., and M. S. P. Sansom. 2001. Amino acid distributions in integral membrane protein structures. Biochim. Biophys. Acta. 1512:1-14.
    • (2001) Biochim. Biophys. Acta , vol.1512 , pp. 1-14
    • Ulmschneider, M.B.1    Sansom, M.S.P.2
  • 68
    • 16344390562 scopus 로고    scopus 로고
    • Properties of integral membrane protein structures: Derivation of an implicit membrane potential
    • Ulmschneider, M. B., M. S. P. Sansom, and A. Di Nola. 2005. Properties of integral membrane protein structures: derivation of an implicit membrane potential. Proteins. 59:252-265.
    • (2005) Proteins , vol.59 , pp. 252-265
    • Ulmschneider, M.B.1    Sansom, M.S.P.2    Di Nola, A.3
  • 70
    • 0242659352 scopus 로고    scopus 로고
    • Protein-lipid interactions studied with designed transmembrane peptides: Role of hydrophobic matching and interfacial anchoring
    • de Planque, M. R. R., and J. A. Killian. 2003. Protein-lipid interactions studied with designed transmembrane peptides: role of hydrophobic matching and interfacial anchoring. Mol. Membr. Biol. 20:271-284.
    • (2003) Mol. Membr. Biol. , vol.20 , pp. 271-284
    • De Planque, M.R.R.1    Killian, J.A.2
  • 71
    • 0242405501 scopus 로고    scopus 로고
    • Synthetic peptides as models for intrinsic membrane proteins
    • Killian, J. A. 2003. Synthetic peptides as models for intrinsic membrane proteins. FEBS Lett. 555:134-138.
    • (2003) FEBS Lett. , vol.555 , pp. 134-138
    • Killian, J.A.1
  • 73
    • 0037168311 scopus 로고    scopus 로고
    • Molecular dynamics simulations of sodium dodecyl sulfate micelle in water: The behavior of water
    • Bruce, C. D., S. Senapati, M. L. Berkowitz, L. Perera, and M. D. E. Forbes. 2002. Molecular dynamics simulations of sodium dodecyl sulfate micelle in water: the behavior of water. J. Phys. Chem. B. 106:10902-10907.
    • (2002) J. Phys. Chem. B , vol.106 , pp. 10902-10907
    • Bruce, C.D.1    Senapati, S.2    Berkowitz, M.L.3    Perera, L.4    Forbes, M.D.E.5
  • 74
    • 0037129516 scopus 로고    scopus 로고
    • Molecular dynamics simulation of sodium dodecyl sulfate micelle in water: Micellar structural characteristics and counterion distribution
    • Bruce, C. D., M. L. Berkowitz, L. Perera, and M. D. E. Forbes. 2002. Molecular dynamics simulation of sodium dodecyl sulfate micelle in water: micellar structural characteristics and counterion distribution. J. Phys. Chem. B. 106:3788-3793.
    • (2002) J. Phys. Chem. B. , vol.106 , pp. 3788-3793
    • Bruce, C.D.1    Berkowitz, M.L.2    Perera, L.3    Forbes, M.D.E.4
  • 75
    • 0033718963 scopus 로고    scopus 로고
    • Molecular dynamics simulations of octyl glucoside micelles: Structural properties
    • Bogusz, S., R. M. Venable, and R. W. Pastor. 2000. Molecular dynamics simulations of octyl glucoside micelles: structural properties. J. Phys. Chem. B. 104:5462-5470.
    • (2000) J. Phys. Chem. B , vol.104 , pp. 5462-5470
    • Bogusz, S.1    Venable, R.M.2    Pastor, R.W.3
  • 76
    • 0035818094 scopus 로고    scopus 로고
    • Molecular dynamics simulations of octyl glucoside micelles: Dynamic properties
    • Bogusz, S., R. M. Venable, and R. W. Pastor. 2001. Molecular dynamics simulations of octyl glucoside micelles: dynamic properties. J. Phys. Chem. B. 105:8312-8321.
    • (2001) J. Phys. Chem. B , vol.105 , pp. 8312-8321
    • Bogusz, S.1    Venable, R.M.2    Pastor, R.W.3
  • 77
    • 27744527489 scopus 로고    scopus 로고
    • Unfolding and extraction of a transmembrane α-helical peptide: Dynamic force spectroscopy and molecular dynamics simulations
    • Antoranz-Contera, S., V. Lemaitre, M. R. de Planque, A. Watts, and J. F. Ryan. 2005. Unfolding and extraction of a transmembrane α-helical peptide: dynamic force spectroscopy and molecular dynamics simulations. Biophys. J. 89:3129-3140.
    • (2005) Biophys. J. , vol.89 , pp. 3129-3140
    • Antoranz-Contera, S.1    Lemaitre, V.2    De Planque, M.R.3    Watts, A.4    Ryan, J.F.5
  • 79
    • 0034284386 scopus 로고    scopus 로고
    • How proteins adapt to a membrane-water interface
    • Killian, J. A., and G. von Heijne. 2000. How proteins adapt to a membrane-water interface. Trends Biochem. Sci. 25:429-434.
    • (2000) Trends Biochem. Sci. , vol.25 , pp. 429-434
    • Killian, J.A.1    Von Heijne, G.2
  • 80
    • 0037671392 scopus 로고    scopus 로고
    • Molecular dynamics simulations of the bacterial outer membrane protein FhuA: A comparative study of the ferrichrome-free and bound states
    • Faraldo-Gómez, J. D., G. R. Smith, and M. S. P. Sansom. 2003. Molecular dynamics simulations of the bacterial outer membrane protein FhuA: a comparative study of the ferrichrome-free and bound states. Biophys. J. 85:1-15.
    • (2003) Biophys. J. , vol.85 , pp. 1-15
    • Faraldo-Gómez, J.D.1    Smith, G.R.2    Sansom, M.S.P.3
  • 82
    • 0042931286 scopus 로고    scopus 로고
    • Sequence motifs, polar interactions and conformational changes in membrane proteins
    • Curran, A. R., and D. Engelman. 2003. Sequence motifs, polar interactions and conformational changes in membrane proteins. Curr. Opin. Struct. Biol. 13:412-417.
    • (2003) Curr. Opin. Struct. Biol. , vol.13 , pp. 412-417
    • Curran, A.R.1    Engelman, D.2
  • 83
    • 3142747401 scopus 로고    scopus 로고
    • Direct simulation of transmembrane helix association: Role of asparagines
    • Stockner, T., W. L. Ash, J. L. MacCallum, and D. P. Tieleman. 2004. Direct simulation of transmembrane helix association: role of asparagines. Biophys. J. 87:1650-1656.
    • (2004) Biophys. J. , vol.87 , pp. 1650-1656
    • Stockner, T.1    Ash, W.L.2    MacCallum, J.L.3    Tieleman, D.P.4
  • 84
    • 0037470691 scopus 로고    scopus 로고
    • Ab initio folding simulation of the Trp-cage mini-protein approaches NMR resolution
    • Chowdhury, S., M. C. Lee, G. Xiong, and Y. Duan. 2003. Ab initio folding simulation of the Trp-cage mini-protein approaches NMR resolution. J. Mol. Biol. 327:711-717.
    • (2003) J. Mol. Biol. , vol.327 , pp. 711-717
    • Chowdhury, S.1    Lee, M.C.2    Xiong, G.3    Duan, Y.4
  • 85
    • 18744403982 scopus 로고    scopus 로고
    • Interfacial folding and membrane insertion of designed peptides studied by molecular dynamics simulations
    • Im, W., and C. L. Brooks. 2005. Interfacial folding and membrane insertion of designed peptides studied by molecular dynamics simulations. Proc. Natl. Acad. Sci. USA. 102:6771-6776.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 6771-6776
    • Im, W.1    Brooks, C.L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.