메뉴 건너뛰기




Volumn 87, Issue 6, 2004, Pages 4065-4074

A model membrane protein for binding volatile anesthetics

Author keywords

[No Author keywords available]

Indexed keywords

AMPHOPHILE; HALOTHANE; INHALATION ANESTHETIC AGENT; ION CHANNEL; MEMBRANE PROTEIN; RECEPTOR PROTEIN;

EID: 10044264645     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1529/biophysj.104.051045     Document Type: Article
Times cited : (13)

References (45)
  • 1
    • 33847057861 scopus 로고
    • Synchrotron x-ray-diffraction study of liquid surfaces
    • Als-Nielsen, J., and P. S. Pershan. 1983. Synchrotron x-ray-diffraction study of liquid surfaces. Nucl. Instrum. Methods. 208:545-548.
    • (1983) Nucl. Instrum. Methods , vol.208 , pp. 545-548
    • Als-Nielsen, J.1    Pershan, P.S.2
  • 2
    • 0033358239 scopus 로고    scopus 로고
    • Neutron scattering in structural biology and biomolecular materials
    • Blasie, J. K., and P. Timmins. 1999. Neutron scattering in structural biology and biomolecular materials. MRS Bull. 24:40-47.
    • (1999) MRS Bull. , vol.24 , pp. 40-47
    • Blasie, J.K.1    Timmins, P.2
  • 3
    • 0000096033 scopus 로고
    • Capillary waves on the surface of simple liquids measured by x-ray reflectivity
    • Braslau, A., P. S. Pershan, G. Swislow, B. M. Ocko, and J. Als-Nielsen. 1988. Capillary waves on the surface of simple liquids measured by x-ray reflectivity. Phys. Rev. A. 38:2457-2470.
    • (1988) Phys. Rev. A , vol.38 , pp. 2457-2470
    • Braslau, A.1    Pershan, P.S.2    Swislow, G.3    Ocko, B.M.4    Als-Nielsen, J.5
  • 4
    • 0031027931 scopus 로고    scopus 로고
    • The lateral pressure profile in membranes: A physical mechanism of general anesthesia
    • Cantor, R. S. 1997. The lateral pressure profile in membranes: a physical mechanism of general anesthesia. Biochemistry. 36:2339-2344.
    • (1997) Biochemistry , vol.36 , pp. 2339-2344
    • Cantor, R.S.1
  • 5
    • 0345686447 scopus 로고    scopus 로고
    • Identification of nicotinic acetylcholine receptor amino acids photo-labeled by the volatile anesthetic halothane
    • Chiara, D. C., L. J. Dangott, R. G. Eckenhoff, and J. B. Cohen. 2003. Identification of nicotinic acetylcholine receptor amino acids photo-labeled by the volatile anesthetic halothane. Biochemistry. 42:13457-13467.
    • (2003) Biochemistry , vol.42 , pp. 13457-13467
    • Chiara, D.C.1    Dangott, L.J.2    Eckenhoff, R.G.3    Cohen, J.B.4
  • 6
    • 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
  • 9
    • 0031459734 scopus 로고    scopus 로고
    • Molecular interactions between inhaled anesthetics and proteins
    • Eckenhoff, R. G., and J. S. Johansson. 1997. Molecular interactions between inhaled anesthetics and proteins. Pharmacol. Rev. 49:343-367.
    • (1997) Pharmacol. Rev. , vol.49 , pp. 343-367
    • Eckenhoff, R.G.1    Johansson, J.S.2
  • 10
    • 0028140369 scopus 로고
    • Molecular and cellular mechanisms of general-anesthesia
    • Franks, N. P., and W. R. Lieb. 1994. Molecular and cellular mechanisms of general-anesthesia. Nature. 367:607-614.
    • (1994) Nature , vol.367 , pp. 607-614
    • Franks, N.P.1    Lieb, W.R.2
  • 11
    • 18244389816 scopus 로고    scopus 로고
    • Which molecular targets are most relevant to general anaesthesia?
    • Franks, N. P., and W. R. Lieb. 1998. Which molecular targets are most relevant to general anaesthesia? Toxicol. Lett. 101:1-8.
    • (1998) Toxicol. Lett. , vol.101 , pp. 1-8
    • Franks, N.P.1    Lieb, W.R.2
  • 12
    • 0035969998 scopus 로고    scopus 로고
    • Polar side chains drive the association of model transmembrane peptides
    • Gratkowski, H., J. D. Lear, and W. F. DeGrado. 2001. Polar side chains drive the association of model transmembrane peptides. Proc. Natl. Acad. Sci. USA. 98:880-885.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 880-885
    • Gratkowski, H.1    Lear, J.D.2    DeGrado, W.F.3
  • 14
    • 0026320893 scopus 로고
    • Phases of phosphatidyl ethanolamine monolayers studied by synchrotron x-ray scattering
    • Helm, C. A., P. Tippmannkrayer, H. Mohwald, J. Als-Nielsen, and K. Kjaer. 1991. Phases of phosphatidyl ethanolamine monolayers studied by synchrotron x-ray scattering. Biophys. J. 60:1457-1476.
    • (1991) Biophys. J. , vol.60 , pp. 1457-1476
    • Helm, C.A.1    Tippmannkrayer, P.2    Mohwald, H.3    Als-Nielsen, J.4    Kjaer, K.5
  • 16
    • 10044283861 scopus 로고    scopus 로고
    • Synthetic β-helical bundles as tools for defining the structural features of volatile general anesthetic binding sites on protein targets
    • Johansson, J. S. 2001. Synthetic β-helical bundles as tools for defining the structural features of volatile general anesthetic binding sites on protein targets. Recent Res. Dev. Biophys. Chem. 2:37-52.
    • (2001) Recent Res. Dev. Biophys. Chem. , vol.2 , pp. 37-52
    • Johansson, J.S.1
  • 17
    • 0037406180 scopus 로고    scopus 로고
    • Noninactivating tandem pore domain potassium channels as attractive targets for general anesthetics
    • Johansson, J. S. 2003. Noninactivating tandem pore domain potassium channels as attractive targets for general anesthetics. Anesth. Analg. 96:1248-1250.
    • (2003) Anesth. Analg. , vol.96 , pp. 1248-1250
    • Johansson, J.S.1
  • 18
    • 0032477890 scopus 로고    scopus 로고
    • A designed cavity in the hydrophobic core of a four-a-helix bundle improves volatile anesthetic binding affinity
    • Johansson, J. S., B. R. Gibney, F. Rabanal, K. S. Reddy, and P. L. Dutton. 1998. A designed cavity in the hydrophobic core of a four-a-helix bundle improves volatile anesthetic binding affinity. Biochemistry. 37:1421-1429.
    • (1998) Biochemistry , vol.37 , pp. 1421-1429
    • Johansson, J.S.1    Gibney, B.R.2    Rabanal, F.3    Reddy, K.S.4    Dutton, P.L.5
  • 19
    • 0034077948 scopus 로고    scopus 로고
    • A designed four-α-helix bundle that binds the volatile general anesthetic halothane with high affinity
    • Johansson, J. S., D. Scharf, L. A. Davies, K. S. Reddy, and R. G. Eckenhoff. 2000. A designed four-α-helix bundle that binds the volatile general anesthetic halothane with high affinity. Biophys. J. 78:982-993.
    • (2000) Biophys. J. , vol.78 , pp. 982-993
    • Johansson, J.S.1    Scharf, D.2    Davies, L.A.3    Reddy, K.S.4    Eckenhoff, R.G.5
  • 20
    • 0029949344 scopus 로고    scopus 로고
    • Minimum structural requirement for an inhalational anesthetic binding site on a protein target
    • Johansson, J. S., and R. G. Eckenhoff. 1996. Minimum structural requirement for an inhalational anesthetic binding site on a protein target. Biochim. Biophys. Acta. 1290:63-68.
    • (1996) Biochim. Biophys. Acta , vol.1290 , pp. 63-68
    • Johansson, J.S.1    Eckenhoff, R.G.2
  • 21
    • 0029122365 scopus 로고
    • Binding of halothane to serum albumin demonstrated by using tryptophan fluorescence
    • Johansson, J. S., R. G. Eckenhoff, and P. L. Dutton. 1995. Binding of halothane to serum albumin demonstrated by using tryptophan fluorescence. Anesthesiology. 83:316-324.
    • (1995) Anesthesiology , vol.83 , pp. 316-324
    • Johansson, J.S.1    Eckenhoff, R.G.2    Dutton, P.L.3
  • 22
    • 0030425315 scopus 로고    scopus 로고
    • Binding of the volatile anesthetic halothane to the hydrophobic core of a tetra-α-helix-bundle protein
    • Johansson, J. S., F. Rabanal, and P. L. Dutton. 1996. Binding of the volatile anesthetic halothane to the hydrophobic core of a tetra-α-helix- bundle protein. J. Pharmacol. Exp. Ther. 279:56-61.
    • (1996) J. Pharmacol. Exp. Ther. , vol.279 , pp. 56-61
    • Johansson, J.S.1    Rabanal, F.2    Dutton, P.L.3
  • 23
    • 0033567181 scopus 로고    scopus 로고
    • General anaesthetic actions on ligand-gated ion channels
    • Krasowski, M. D., and N. L. Harrison. 1999. General anaesthetic actions on ligand-gated ion channels. Cell. Mol. Life Sci. 55:1278-1303.
    • (1999) Cell. Mol. Life Sci. , vol.55 , pp. 1278-1303
    • Krasowski, M.D.1    Harrison, N.L.2
  • 24
    • 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
  • 25
    • 0027360326 scopus 로고
    • Influence of surface-chemistry on the structural organization of monomolecular protein layers adsorbed to functionalized aqueous interfaces
    • Lösche, M., M. Piepenstock, A. Diederich, T. Grunewald, K. Kjaer, and D. Vaknin. 1993. Influence of surface-chemistry on the structural organization of monomolecular protein layers adsorbed to functionalized aqueous interfaces. Biophys. J. 65:2160-2177.
    • (1993) Biophys. J. , vol.65 , pp. 2160-2177
    • Lösche, M.1    Piepenstock, M.2    Diederich, A.3    Grunewald, T.4    Kjaer, K.5    Vaknin, D.6
  • 26
    • 0030816685 scopus 로고    scopus 로고
    • Mechanism of helix induction by trifluoroethanol: A framework for extrapolating the helix-forming properties of peptides from trifluoroethanol/ water mixtures back to water
    • Luo, P. Z., and R. L. Baldwin. 1997. Mechanism of helix induction by trifluoroethanol: a framework for extrapolating the helix-forming properties of peptides from trifluoroethanol/water mixtures back to water. Biochemistry. 36:8413-8421.
    • (1997) Biochemistry , vol.36 , pp. 8413-8421
    • Luo, P.Z.1    Baldwin, R.L.2
  • 27
    • 0037177228 scopus 로고    scopus 로고
    • Role of aromatic side chains in the binding of volatile general anesthetics to a four-α-helix bundle
    • Manderson, G. A., and J. S. Johansson. 2002. Role of aromatic side chains in the binding of volatile general anesthetics to a four-α-helix bundle. Biochemistry. 41:4080-4087.
    • (2002) Biochemistry , vol.41 , pp. 4080-4087
    • Manderson, G.A.1    Johansson, J.S.2
  • 28
    • 0030896261 scopus 로고    scopus 로고
    • The rational design of allosteric interactions in a monomeric protein and its applications to the construction of biosensors
    • Marvin, J. S., E. E. Corcoran, N. A. Hattangadi, J. V. Zhang, S. A. Gere, and H. W. Hellinga. 1997. The rational design of allosteric interactions in a monomeric protein and its applications to the construction of biosensors. Proc. Natl. Acad. Sci. USA. 94:4366-4371.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 4366-4371
    • Marvin, J.S.1    Corcoran, E.E.2    Hattangadi, N.A.3    Zhang, J.V.4    Gere, S.A.5    Hellinga, H.W.6
  • 29
    • 0043166158 scopus 로고    scopus 로고
    • Direct analysis of protein sedimentation equilibrium in detergent solutions without density matching
    • Noy, D., J. R. Calhoun, and J. D. Lear. 2003. Direct analysis of protein sedimentation equilibrium in detergent solutions without density matching. Anal. Biochem. 320:185-192.
    • (2003) Anal. Biochem. , vol.320 , pp. 185-192
    • Noy, D.1    Calhoun, J.R.2    Lear, J.D.3
  • 30
    • 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
  • 31
    • 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
  • 32
    • 0015977588 scopus 로고
    • The interpretation of protein structures: Total volume, group volume distributions and packing density
    • Richards, F. M. 1974. The interpretation of protein structures: total volume, group volume distributions and packing density. J. Mol. Biol. 82:1-14.
    • (1974) J. Mol. Biol. , vol.82 , pp. 1-14
    • Richards, F.M.1
  • 33
    • 0041352143 scopus 로고    scopus 로고
    • Acetylcholine binding protein (AChBP): A secreted glial protein that provides a high-resolution model for the extracellular domain of pentameric ligand-gated ion channels
    • Sixma, T. K., and A. B. Smit. 2003. Acetylcholine binding protein (AChBP): a secreted glial protein that provides a high-resolution model for the extracellular domain of pentameric ligand-gated ion channels. Annu. Rev. Biophys. Biomembr. 32:311-334.
    • (2003) Annu. Rev. Biophys. Biomembr. , vol.32 , pp. 311-334
    • Sixma, T.K.1    Smit, A.B.2
  • 35
    • 0036086351 scopus 로고    scopus 로고
    • The α-helix and the organization and gating of channels
    • Spencer, R. H., and D. C. Rees. 2002. The α-helix and the organization and gating of channels. Annu. Rev. Biophys. Biomembr. 31:207-233.
    • (2002) Annu. Rev. Biophys. Biomembr. , vol.31 , pp. 207-233
    • Spencer, R.H.1    Rees, D.C.2
  • 36
    • 0034513345 scopus 로고    scopus 로고
    • X-ray scattering studies of maquette peptide monolayers. 1. Reflectivity and grazing incidence diffraction at the air/water interface
    • Strzalka, J. W., X. Chen, C. C. Moser, P. L. Dutton, B. M. Ocko, and J. K. Blasie. 2000. X-ray scattering studies of maquette peptide monolayers. 1. Reflectivity and grazing incidence diffraction at the air/water interface. Langmuir. 16:10404-10418.
    • (2000) Langmuir , vol.16 , pp. 10404-10418
    • Strzalka, J.W.1    Chen, X.2    Moser, C.C.3    Dutton, P.L.4    Ocko, B.M.5    Blasie, J.K.6
  • 37
    • 41349097474 scopus 로고    scopus 로고
    • Resonant x-ray reflectivity from a bromine-labeled fatty acid Langmuir monolayer
    • In press
    • Strzalka, J., E. DiMasi, I. Kuzmenko, T. Gog, and J. K. Blasie. 2004a. Resonant x-ray reflectivity from a bromine-labeled fatty acid Langmuir monolayer. Phys. Rev. E. In press.
    • (2004) Phys. Rev. E
    • Strzalka, J.1    DiMasi, E.2    Kuzmenko, I.3    Gog, T.4    Blasie, J.K.5
  • 38
    • 37649031208 scopus 로고    scopus 로고
    • Specular neutron reflectivity and the structure of artificial protein maquettes vectorially oriented at interfaces
    • In press
    • Strzalka, J., B. R. Gibney, S. Satija, and J. K. Blasie. 2004b. Specular neutron reflectivity and the structure of artificial protein maquettes vectorially oriented at interfaces. Phys. Rev. E. In press.
    • (2004) Phys. Rev. E
    • Strzalka, J.1    Gibney, B.R.2    Satija, S.3    Blasie, J.K.4
  • 39
    • 0036286167 scopus 로고    scopus 로고
    • NMR structures of the second transmembrane domain of the human glycine receptor α1 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 α1 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
    • 0034711760 scopus 로고    scopus 로고
    • Secondary structure, orientation, oligomerization, and lipid interactions of the transmembrane domain of influenza hemagglutinin
    • Tatulian, S. A., and L. K. Tamm. 2000. Secondary structure, orientation, oligomerization, and lipid interactions of the transmembrane domain of influenza hemagglutinin. Biochemistry. 39:496-507.
    • (2000) Biochemistry , vol.39 , pp. 496-507
    • Tatulian, S.A.1    Tamm, L.K.2
  • 41
    • 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. BBA Biomembr. 1512:1-14.
    • (2001) BBA Biomembr. , vol.1512 , pp. 1-14
    • Ulmschneider, M.B.1    Sansom, M.S.P.2
  • 42
    • 0028921479 scopus 로고
    • Acetylcholine-receptor channel imaged in the open state
    • Unwin, N. 1995. Acetylcholine-receptor channel imaged in the open state. Nature. 373:37-43.
    • (1995) Nature , vol.373 , pp. 37-43
    • Unwin, N.1
  • 43
    • 0034081258 scopus 로고    scopus 로고
    • NMR study of volatile anesthetic binding to nicotinic acetylcholine receptors
    • Xu, Y., T. Seto, P. Tang, and L. Firestone. 2000. NMR study of volatile anesthetic binding to nicotinic acetylcholine receptors. Biophys. J. 78: 746-751.
    • (2000) Biophys. J. , vol.78 , pp. 746-751
    • Xu, Y.1    Seto, T.2    Tang, P.3    Firestone, L.4
  • 44
    • 3142662537 scopus 로고    scopus 로고
    • Amphiphilic 4-helix bundles designed for biomolecular materials applications
    • Ye, S., J. W. Strzalka, B. M. Discher, D. Noy, S. Zheng, P. L. Dutton, and J. K. Blasie. 2004. Amphiphilic 4-helix bundles designed for biomolecular materials applications. Langmuir. 20:5897-5904.
    • (2004) Langmuir , vol.20 , pp. 5897-5904
    • Ye, S.1    Strzalka, J.W.2    Discher, B.M.3    Noy, D.4    Zheng, S.5    Dutton, P.L.6    Blasie, J.K.7
  • 45
    • 0037382308 scopus 로고    scopus 로고
    • Comparative structural studies of VPU peptides in phospholipid monolayers by x-ray scattering
    • Zheng, S., J. Strzalka, D. H. Jones, S. J. Opella, and J. K. Blasie. 2003. Comparative structural studies of VPU peptides in phospholipid monolayers by x-ray scattering. Biophys. J. 84:2393-2415.
    • (2003) Biophys. J. , vol.84 , pp. 2393-2415
    • Zheng, S.1    Strzalka, J.2    Jones, D.H.3    Opella, S.J.4    Blasie, J.K.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.