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Volumn 30, Issue 1, 1998, Pages 61-73

Exploring hydrophobic sites in proteins with xenon or krypton

Author keywords

Hydrophobic cavity; Krypton; Protein ligand binding; Xenon

Indexed keywords

COLLAGENASE; CUTINASE; ENDOTOXIN; KRYPTON; LYSOZYME; OUTER MEMBRANE PROTEIN; PANCREATIC ELASTASE; SUBTILISIN; URATE OXIDASE; XENON;

EID: 0002306796     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-0134(19980101)30:1<61::AID-PROT6>3.0.CO;2-N     Document Type: Article
Times cited : (173)

References (74)
  • 2
    • 0029012163 scopus 로고
    • Crystal structure of the ligand binding domain of the human nuclear receptor RXRα
    • Bourguet, W., Ruff, M., Chambon, P., Gronemeyer, H., Moras, D. Crystal structure of the ligand binding domain of the human nuclear receptor RXRα. Nature 375:377-382, 1995.
    • (1995) Nature , vol.375 , pp. 377-382
    • Bourguet, W.1    Ruff, M.2    Chambon, P.3    Gronemeyer, H.4    Moras, D.5
  • 4
    • 84901961522 scopus 로고
    • Slow-coding protocols for crystallographic refinement by simulated Annealing
    • Brünger, A.T., Krukowski, A., Erickson, J.W. Slow-coding protocols for crystallographic refinement by simulated Annealing. Acta Crystallogr. A46:585-593, 1990.
    • (1990) Acta Crystallogr. , vol.A46 , pp. 585-593
    • Brünger, A.T.1    Krukowski, A.2    Erickson, J.W.3
  • 5
    • 0000625192 scopus 로고
    • CCP4 Collaborative Computational Project, Number 4
    • CCP4 Collaborative Computational Project, Number 4. Acta Crystallogr. D 50:760-764, 1994.
    • (1994) Acta Crystallogr. D , vol.50 , pp. 760-764
  • 6
  • 8
    • 0000862156 scopus 로고
    • Equilibrium distribution of radio-xenon in tissue: Xenon-hemoglobin association curve
    • Conn, H.L. Equilibrium distribution of radio-xenon in tissue: Xenon-hemoglobin association curve. J. Appl. Physiol. 16:1065-1070, 1961.
    • (1961) J. Appl. Physiol. , vol.16 , pp. 1065-1070
    • Conn, H.L.1
  • 9
    • 0000538815 scopus 로고
    • Analytical molecular surfaces calculation
    • Connolly, M.L. Analytical molecular surfaces calculation. J. Appl. Cryst. 16:548-558, 1983.
    • (1983) J. Appl. Cryst. , vol.16 , pp. 548-558
    • Connolly, M.L.1
  • 10
    • 0001101644 scopus 로고
    • The anesthetic properties of xenon in human and animal beings, with additional observations on krypton
    • Cullen, S.C., Gross, E.G. The anesthetic properties of xenon in human and animal beings, with additional observations on krypton. Science 113:580-582, 1951.
    • (1951) Science , vol.113 , pp. 580-582
    • Cullen, S.C.1    Gross, E.G.2
  • 11
    • 0014966029 scopus 로고
    • The thermodynamics of absorption of xenon by myoglobin
    • Ewing, J.G., Maestas, S. The thermodynamics of absorption of xenon by myoglobin. J. Phys. Chem. 74:2341-2344, 1970.
    • (1970) J. Phys. Chem. , vol.74 , pp. 2341-2344
    • Ewing, J.G.1    Maestas, S.2
  • 12
    • 0003356308 scopus 로고
    • The current role of inert gases in the search for anesthesia mechanisms
    • Featherstone, R.M., Muehlbaecher, C.A. The current role of inert gases in the search for anesthesia mechanisms. Pharmacol. Rev. 15:97-121, 1963.
    • (1963) Pharmacol. Rev. , vol.15 , pp. 97-121
    • Featherstone, R.M.1    Muehlbaecher, C.A.2
  • 14
    • 0029882583 scopus 로고    scopus 로고
    • Access of ligands to cavities within the core of a protein is rapid
    • Feher, V.A., Baldwin, E.P., Dahlquist, F.W. Access of ligands to cavities within the core of a protein is rapid. Nature Struct. Biol. 3:516-521, 1996.
    • (1996) Nature Struct. Biol. , vol.3 , pp. 516-521
    • Feher, V.A.1    Baldwin, E.P.2    Dahlquist, F.W.3
  • 15
    • 0001129836 scopus 로고
    • Bent crystal, bent multilayer optics on a multipole wiggler line for an X-ray diffractometer with an imaging plate detector
    • Fourme, R., Dhez, P., Benoit, J.-P., Kahn, R., Dubuisson, J.-M., Besson, P., Frouin, J. Bent crystal, bent multilayer optics on a multipole wiggler line for an X-ray diffractometer with an imaging plate detector. Rev. Sci. Instrum. 63:982-987, 1992.
    • (1992) Rev. Sci. Instrum. , vol.63 , pp. 982-987
    • Fourme, R.1    Dhez, P.2    Benoit, J.-P.3    Kahn, R.4    Dubuisson, J.-M.5    Besson, P.6    Frouin, J.7
  • 16
    • 0023221417 scopus 로고
    • What is the molecular nature of general anaesthetic target sites?
    • Franks, N.P., Lieb, W.R. What is the molecular nature of general anaesthetic target sites? Trends Pharmacol. Sci. 8:169-174, 1987.
    • (1987) Trends Pharmacol. Sci. , vol.8 , pp. 169-174
    • Franks, N.P.1    Lieb, W.R.2
  • 17
    • 0028140369 scopus 로고
    • Molecular and cellular mechanisms of general anaesthesia
    • Franks, N.P., Lieb, W.R. Molecular and cellular mechanisms of general anaesthesia. Nature 367:607-614, 1994.
    • (1994) Nature , vol.367 , pp. 607-614
    • Franks, N.P.1    Lieb, W.R.2
  • 18
    • 0022333121 scopus 로고
    • Stereochemically restrained refinement of macromolecular structures
    • Hendrickson, W.A., Konnert, J.H. Stereochemically restrained refinement of macromolecular structures. Methods Enzymol. 115:252-270, 1985.
    • (1985) Methods Enzymol. , vol.115 , pp. 252-270
    • Hendrickson, W.A.1    Konnert, J.H.2
  • 19
    • 85005687495 scopus 로고
    • The free energy of xenon binding to myoglobin from molecular dynamics simulation
    • Hermans, J., Shankar, S. The free energy of xenon binding to myoglobin from molecular dynamics simulation. Isr. J. Chem. 27:225-227, 1986.
    • (1986) Isr. J. Chem. , vol.27 , pp. 225-227
    • Hermans, J.1    Shankar, S.2
  • 20
    • 0028274954 scopus 로고
    • Intramolecular cavities in globular proteins
    • Hubbard, S.J., Gross, K.H., Argos, P. Intramolecular cavities in globular proteins. Protein Eng. 7:613-626, 1994.
    • (1994) Protein Eng. , vol.7 , pp. 613-626
    • Hubbard, S.J.1    Gross, K.H.2    Argos, P.3
  • 21
    • 0015237085 scopus 로고
    • On the nature of the protein interior
    • Klapper, M.H. On the nature of the protein interior. Biochim. Biophys. Acta 229:557-566, 1971.
    • (1971) Biochim. Biophys. Acta , vol.229 , pp. 557-566
    • Klapper, M.H.1
  • 22
    • 0030589519 scopus 로고    scopus 로고
    • Properties of the protein matrix revealed by the free energy of cavity formation
    • Kocher, J.P., Prévost, M., Wodak, S.J., Lee, B. Properties of the protein matrix revealed by the free energy of cavity formation. Structure 4:1517-1529, 1996.
    • (1996) Structure , vol.4 , pp. 1517-1529
    • Kocher, J.P.1    Prévost, M.2    Wodak, S.J.3    Lee, B.4
  • 23
    • 0029911269 scopus 로고    scopus 로고
    • Photosystem I at 4Å resolution: A joint photosynthetic reaction center and core antenna system
    • Krauß, N., Schubert, W.D., Klukas, O., Frome, P., Witt, H.T., Saenger, W. Photosystem I at 4Å resolution: A joint photosynthetic reaction center and core antenna system. Nature Struct. Biol. 3:965-973, 1996.
    • (1996) Nature Struct. Biol. , vol.3 , pp. 965-973
    • Krauß, N.1    Schubert, W.D.2    Klukas, O.3    Frome, P.4    Witt, H.T.5    Saenger, W.6
  • 24
    • 0029140564 scopus 로고
    • The influence of temperature on lysozyme crystals. Structure and dynamics of protein and water
    • Kurinov, I.V., Harrison, R.W. The influence of temperature on lysozyme crystals. Structure and dynamics of protein and water. Acta Crystallogr. D 51:98-109, 1995.
    • (1995) Acta Crystallogr. D , vol.51 , pp. 98-109
    • Kurinov, I.V.1    Harrison, R.W.2
  • 27
    • 0028284860 scopus 로고
    • Brain imaging in late-life psychosis
    • Lesser, I.M. Brain imaging in late-life psychosis. Curr. Opin. Psychiatry 7:354-357, 1994.
    • (1994) Curr. Opin. Psychiatry , vol.7 , pp. 354-357
    • Lesser, I.M.1
  • 28
    • 0029669956 scopus 로고    scopus 로고
    • Structure of the mosquitocidal δ-endotoxin CytB from Bacillus thuringiensis sp. kyushuensis and implications for membrane pore formation
    • Li, J., Pandelakis, A., Koni, P.A., Ellar, D.J. Structure of the mosquitocidal δ-endotoxin CytB from Bacillus thuringiensis sp. kyushuensis and implications for membrane pore formation. J. Mol. Biol. 257:129-152, 1996.
    • (1996) J. Mol. Biol. , vol.257 , pp. 129-152
    • Li, J.1    Pandelakis, A.2    Koni, P.A.3    Ellar, D.J.4
  • 29
    • 0028082495 scopus 로고
    • Crystallisation and preliminary X-ray investigation of a recombinant outer membrane protein from Neisseria meningitidis
    • Li de la Sierra, I., Prangé, T., Fourme, R., Padrón, G., Fuentes, P., Musacchio, A., Madrazo, J. Crystallisation and preliminary X-ray investigation of a recombinant outer membrane protein from Neisseria meningitidis. J. Mol. Biol. 235:1154-1155, 1994.
    • (1994) J. Mol. Biol. , vol.235 , pp. 1154-1155
    • Li De La Sierra, I.1    Prangé, T.2    Fourme, R.3    Padrón, G.4    Fuentes, P.5    Musacchio, A.6    Madrazo, J.7
  • 30
    • 0031591386 scopus 로고    scopus 로고
    • Molecular structure of the Lipoamide dehydrogenase domain of a surface antigen from Neisseria meningitidis
    • Li de la Sierra, I., Pernot, L., Prangé, T., Saludjian, P., Schiltz, M., Fourme, R., Padrón, G. Molecular structure of the Lipoamide dehydrogenase domain of a surface antigen from Neisseria meningitidis. J. Mol. Biol. 269:129-141, 1997.
    • (1997) J. Mol. Biol. , vol.269 , pp. 129-141
    • Li De La Sierra, I.1    Pernot, L.2    Prangé, T.3    Saludjian, P.4    Schiltz, M.5    Fourme, R.6    Padrón, G.7
  • 31
    • 0029911261 scopus 로고    scopus 로고
    • The crystal structure of a five-stranded coiled-coil in COMP: A prototype ion channel?
    • Malashkevich, V.N., Kammerer, R.A., Efimov, V., Schulthess, T., Engel, J. The crystal structure of a five-stranded coiled-coil in COMP: A prototype ion channel? Science 274:761-765, 1996.
    • (1996) Science , vol.274 , pp. 761-765
    • Malashkevich, V.N.1    Kammerer, R.A.2    Efimov, V.3    Schulthess, T.4    Engel, J.5
  • 32
    • 0026583770 scopus 로고
    • Fusarium solani cutinase is a lypolytic enzyme with a catalytic serine accessible to solvent
    • Martinez, C., De Geus, P., Lauwereys, M., Mathissens, G., Cambillau, C. Fusarium solani cutinase is a lypolytic enzyme with a catalytic serine accessible to solvent. Nature 356:615-618, 1992.
    • (1992) Nature , vol.356 , pp. 615-618
    • Martinez, C.1    De Geus, P.2    Lauwereys, M.3    Mathissens, G.4    Cambillau, C.5
  • 33
    • 0027480349 scopus 로고
    • Engineering cystein mutants to obtain crystallographic phases with a cutinase from Fusarium solani pisi
    • Martinez, C., De Geus, P., Lauwereys, M., Mathissens, G., Cambillau, C. Engineering cystein mutants to obtain crystallographic phases with a cutinase from Fusarium solani pisi. Protein Eng. 6:157-165, 1993.
    • (1993) Protein Eng. , vol.6 , pp. 157-165
    • Martinez, C.1    De Geus, P.2    Lauwereys, M.3    Mathissens, G.4    Cambillau, C.5
  • 34
    • 0002104779 scopus 로고
    • Structure of native porcine pancreatic elastase at 1.65Å resolution
    • Meyer, E.F., Cole, G.M., Radhakrishnan, R., Epp, C. Structure of native porcine pancreatic elastase at 1.65Å resolution. Acta Crystallogr. B 44:26-38, 1988.
    • (1988) Acta Crystallogr. B , vol.44 , pp. 26-38
    • Meyer, E.F.1    Cole, G.M.2    Radhakrishnan, R.3    Epp, C.4
  • 35
    • 0022309995 scopus 로고
    • The nature of the site of general anesthesia
    • Miller, K. W. The nature of the site of general anesthesia. Int. Rev. Neurobiol. 27:1-61, 1985.
    • (1985) Int. Rev. Neurobiol. , vol.27 , pp. 1-61
    • Miller, K.W.1
  • 37
    • 0029067489 scopus 로고
    • Specificity of ligand binding in a buried nonpolar cavity of T4 lysozyme: Linkage of dynamics and structural plasticity
    • Morton, A., Matthews, B.W. Specificity of ligand binding in a buried nonpolar cavity of T4 lysozyme: Linkage of dynamics and structural plasticity. Biochemistry 34:8576-8588, 1995.
    • (1995) Biochemistry , vol.34 , pp. 8576-8588
    • Morton, A.1    Matthews, B.W.2
  • 38
    • 0015759816 scopus 로고
    • Dichloromethane and myoglobin function
    • Nunes, A.C., Schoenborn, B.P. Dichloromethane and myoglobin function. Mol. Pharmacol. 9:835-839, 1973.
    • (1973) Mol. Pharmacol. , vol.9 , pp. 835-839
    • Nunes, A.C.1    Schoenborn, B.P.2
  • 39
    • 0002634621 scopus 로고
    • Maximum likelihood refinement of heavy atom parameters
    • "Isomorphous Replacement and Anomalous Scattering." January 25-26, 1991. Wolf, W., Evans, PR., & Leslie, A.G.W. (eds.). Warrington: SERC Daresbury Laboratory
    • Otwinowski, Z. Maximum likelihood refinement of heavy atom parameters. In: "Isomorphous Replacement and Anomalous Scattering." Proceedings of the CCP4 Study Weekend, January 25-26, 1991. Wolf, W., Evans, PR., & Leslie, A.G.W. (eds.). Warrington: SERC Daresbury Laboratory, 1991:80-86.
    • (1991) Proceedings of the CCP4 Study Weekend , pp. 80-86
    • Otwinowski, Z.1
  • 40
    • 0017125288 scopus 로고
    • The structure of subtilopeptidase, 1. X-ray crystallographic data
    • Petsko, G.A., Tsernoglou, D. The structure of subtilopeptidase, 1. X-ray crystallographic data. J. Mol. Biol. 106:453-456, 1976.
    • (1976) J. Mol. Biol. , vol.106 , pp. 453-456
    • Petsko, G.A.1    Tsernoglou, D.2
  • 41
    • 4243823868 scopus 로고    scopus 로고
    • Binding of small electron-dense ligands in large protein cavities
    • XVII Congress and General Assembly of the International Union of Crystallogr., Seattle, WA. Abstract PS04.14.17
    • Quilin, M.L., Baase, W.A., Matthews, B. Binding of small electron-dense ligands in large protein cavities. XVII Congress and General Assembly of the International Union of Crystallogr., Seattle, WA. Abstract PS04.14.17 in: Acta Crystallogr. A52: C-215, 1996.
    • (1996) Acta Crystallogr. , vol.A52
    • Quilin, M.L.1    Baase, W.A.2    Matthews, B.3
  • 42
    • 0017684533 scopus 로고
    • Halothane binds in the adenine-specific niche of crystalline adenylate kinase
    • Sachsenheimer, W., Pai, E.F., Schultz, G.E., Schirmer, R.H. Halothane binds in the adenine-specific niche of crystalline adenylate kinase. FEBS Lett. 79:310-312, 1977.
    • (1977) FEBS Lett. , vol.79 , pp. 310-312
    • Sachsenheimer, W.1    Pai, E.F.2    Schultz, G.E.3    Schirmer, R.H.4
  • 43
    • 6844220094 scopus 로고    scopus 로고
    • Freeze-trapping isomorphous xenon derivatives of protein crystals
    • in press
    • Sauer, O., Schmidt, A., Kratky, C. Freeze-trapping isomorphous xenon derivatives of protein crystals. J. Appl. Cryst., (in press).
    • J. Appl. Cryst.
    • Sauer, O.1    Schmidt, A.2    Kratky, C.3
  • 45
    • 0028736397 scopus 로고
    • On the preparation and X-ray data collection of isomorphous xenon derivatives
    • Schiltz, M., Prangé, T., Fourme, R. On the preparation and X-ray data collection of isomorphous xenon derivatives. J. Appl. Cryst. 27:950-960, 1994.
    • (1994) J. Appl. Cryst. , vol.27 , pp. 950-960
    • Schiltz, M.1    Prangé, T.2    Fourme, R.3
  • 46
    • 0029644248 scopus 로고
    • The catalytic site of serine proteinases as a specific binding cavity for xenon
    • Schiltz, M., Fourme, R., Broutin, I., Prangé, T. The catalytic site of serine proteinases as a specific binding cavity for xenon. Structure 3:309-316, 1995.
    • (1995) Structure , vol.3 , pp. 309-316
    • Schiltz, M.1    Fourme, R.2    Broutin, I.3    Prangé, T.4
  • 47
    • 0030977946 scopus 로고    scopus 로고
    • High-pressure krypton gas and statistical heavy-atom refinement: A successful combination of tools for macromolecular structure determination
    • Schiltz, M., Shepard, W., Fourme, R., Prangé, T., de la Fortelle, E., Bricogne, G. High-pressure krypton gas and statistical heavy-atom refinement: A successful combination of tools for macromolecular structure determination. Acta Crystallogr. D 53:78-92, 1997.
    • (1997) Acta Crystallogr. D , vol.53 , pp. 78-92
    • Schiltz, M.1    Shepard, W.2    Fourme, R.3    Prangé, T.4    De La Fortelle, E.5    Bricogne, G.6
  • 49
    • 0030006891 scopus 로고    scopus 로고
    • Crystal structure of DMSO reductase: Redox-linked changes in molybdopterin coordination
    • Schindelin, H., Kisker, C., Hilton, J., Rajagopalan, K.V., Rees, D.C. Crystal structure of DMSO reductase: Redox-linked changes in molybdopterin coordination. Science 272:1615-1621, 1996.
    • (1996) Science , vol.272 , pp. 1615-1621
    • Schindelin, H.1    Kisker, C.2    Hilton, J.3    Rajagopalan, K.V.4    Rees, D.C.5
  • 50
    • 0013851845 scopus 로고
    • Binding of xenon to horse haemoglobin
    • Schoenborn, B.P. Binding of xenon to horse haemoglobin. Nature 208:760-762, 1965.
    • (1965) Nature , vol.208 , pp. 760-762
    • Schoenborn, B.P.1
  • 51
    • 0014198467 scopus 로고
    • Binding of cyclopropane to sperm whale myoglobin
    • Schoenborn, B.P. Binding of cyclopropane to sperm whale myoglobin. Nature 214:1120-1122, 1967.
    • (1967) Nature , vol.214 , pp. 1120-1122
    • Schoenborn, B.P.1
  • 52
    • 0014284716 scopus 로고
    • Binding of anesthetics to proteins: An X-ray crystallographic investigation
    • Schoenborn, B.P. Binding of anesthetics to proteins: An X-ray crystallographic investigation. Fed. Proc. Fed. Am. Soc. Exp. Biol. 27:888-894, 1968.
    • (1968) Fed. Proc. Fed. Am. Soc. Exp. Biol. , vol.27 , pp. 888-894
    • Schoenborn, B.P.1
  • 53
    • 0014694179 scopus 로고
    • Structure of alkaline metmyoglobin-xenon complex
    • Schoenborn, B.P. Structure of alkaline metmyoglobin-xenon complex. J. Mol. Biol. 45:297-303, 1969.
    • (1969) J. Mol. Biol. , vol.45 , pp. 297-303
    • Schoenborn, B.P.1
  • 55
    • 0013947574 scopus 로고
    • The binding of xenon to sperm whale deoxymyoglobin
    • Schoenborn, B.P., Nobbs, C.L. The binding of xenon to sperm whale deoxymyoglobin. Mol. Pharmacol. 2:495-498, 1966.
    • (1966) Mol. Pharmacol. , vol.2 , pp. 495-498
    • Schoenborn, B.P.1    Nobbs, C.L.2
  • 56
    • 6844230727 scopus 로고
    • Function of the myoglobin molecule as influenced by anesthetic molecules
    • Featherstone, R.M. (ed.). New York: Marcel Dekker
    • Settle, W. Function of the myoglobin molecule as influenced by anesthetic molecules. In: "Guide to Molecular Pharmacology-Toxicology." Featherstone, R.M. (ed.). New York: Marcel Dekker, 1973.
    • (1973) Guide to Molecular Pharmacology-Toxicology
    • Settle, W.1
  • 57
    • 0002268479 scopus 로고
    • Preliminary X-ray data for some new crystalline forms of β-lactoglobulin and hen egg-white lysozyme
    • Steinrauf, L.K. Preliminary X-ray data for some new crystalline forms of β-lactoglobulin and hen egg-white lysozyme. Acta Crystallogr. 12:77-79, 1959.
    • (1959) Acta Crystallogr. , vol.12 , pp. 77-79
    • Steinrauf, L.K.1
  • 59
    • 0020285568 scopus 로고
    • Nuclear magnetic resonance studies of xenon-129 with myoglogin and haemoglobin
    • Tilton, R.F., Kuntz, I.D. Nuclear magnetic resonance studies of xenon-129 with myoglogin and haemoglobin. Biochemistry 21:6850-6857, 1982.
    • (1982) Biochemistry , vol.21 , pp. 6850-6857
    • Tilton, R.F.1    Kuntz, I.D.2
  • 60
    • 0023784241 scopus 로고
    • A structure of sperm whale myoglobin at a nitrogen gas pressure of 145 atmospheres
    • Tilton, R.F., Petsko, G.A. A structure of sperm whale myoglobin at a nitrogen gas pressure of 145 atmospheres. Biochemistry 27:6574-6582, 1988.
    • (1988) Biochemistry , vol.27 , pp. 6574-6582
    • Tilton, R.F.1    Petsko, G.A.2
  • 61
    • 0021766921 scopus 로고
    • Cavities in proteins: Structure of a metmyoglobin-xenon complex solved to 1.9Å
    • Tilton, R.F., Kuntz, I.D., Petsko, G.A. Cavities in proteins: Structure of a metmyoglobin-xenon complex solved to 1.9Å. Biochemistry 23:2849-2857, 1984.
    • (1984) Biochemistry , vol.23 , pp. 2849-2857
    • Tilton, R.F.1    Kuntz, I.D.2    Petsko, G.A.3
  • 63
    • 0024278057 scopus 로고
    • Protein-ligand dynamics. A 96 picosecond simulation of a myoglobin-xenon complex
    • Tilton, R.F., Singh, U.C., Kuntz, I.D., Kollman, P.A. Protein-ligand dynamics. A 96 picosecond simulation of a myoglobin-xenon complex. J. Mol. Biol. 199:195-211, 1988.
    • (1988) J. Mol. Biol. , vol.199 , pp. 195-211
    • Tilton, R.F.1    Singh, U.C.2    Kuntz, I.D.3    Kollman, P.A.4
  • 64
    • 0026242219 scopus 로고
    • Using xenon as a heavy atom for determining phases in sperm whale met-myoglobin
    • Vitali, J., Robbins, A.H., Almo, S.C., Tilton, R.F. Using xenon as a heavy atom for determining phases in sperm whale met-myoglobin. J. Appl. Cryst. 24:931-935, 1991.
    • (1991) J. Appl. Cryst. , vol.24 , pp. 931-935
    • Vitali, J.1    Robbins, A.H.2    Almo, S.C.3    Tilton, R.F.4
  • 66
    • 0028093141 scopus 로고
    • On the probability of finding a water molecule in a non-polar cavity
    • Wolfenden, R., Radzicka, A. On the probability of finding a water molecule in a non-polar cavity. Science 265:936-937, 1994.
    • (1994) Science , vol.265 , pp. 936-937
    • Wolfenden, R.1    Radzicka, A.2
  • 67
    • 0029937870 scopus 로고    scopus 로고
    • Hydrophilicity of cavities in proteins
    • Zhang, L.I., Hermans, J. Hydrophilicity of cavities in proteins. Proteins 24:433-438, 1996.
    • (1996) Proteins , vol.24 , pp. 433-438
    • Zhang, L.I.1    Hermans, J.2
  • 68
    • 0013842370 scopus 로고
    • Binding of xenon to sperm whale myoglobin
    • Schoenborn, B.P., Watson, H.C., Kendrew, J.C. Binding of xenon to sperm whale myoglobin. Nature 207:28-30, 1965.
    • (1965) Nature , vol.207 , pp. 28-30
    • Schoenborn, B.P.1    Watson, H.C.2    Kendrew, J.C.3
  • 69
    • 0015460446 scopus 로고
    • The Membrane Actions of Anesthetics and Tranquilizers
    • Seeman, P. The Membrane Actions of Anesthetics and Tranquilizers. Pharmacol. Rev. 24:583-655, 1972.
    • (1972) Pharmacol. Rev. , vol.24 , pp. 583-655
    • Seeman, P.1
  • 72
    • 6844229662 scopus 로고
    • Influence of Xenon on Protein Hydration as measured by a Microwave Absorption Technique
    • Schoenborn, B.P., Featherstone, R.M., Vogelhut, P.O. Süsskind, C. Influence of Xenon on Protein Hydration as measured by a Microwave Absorption Technique. Nature 202:695-696, 1964.
    • (1964) Nature , vol.202 , pp. 695-696
    • Schoenborn, B.P.1    Featherstone, R.M.2    Vogelhut, P.O.3    Süsskind, C.4
  • 73
    • 0028860335 scopus 로고
    • Channel Inhibition by Alkanols occurs at a Binding Site on the Nicotinic Acetylcholine Receptor
    • Woods, S.C., Tonner, PH., De Armendi, A.J., Bugge, B., Miller, K.W. Channel Inhibition by Alkanols occurs at a Binding Site on the Nicotinic Acetylcholine Receptor. Mol. Pharmacol. 47:121-130, 1995.
    • (1995) Mol. Pharmacol. , vol.47 , pp. 121-130
    • Woods, S.C.1    Tonner, P.H.2    De Armendi, A.J.3    Bugge, B.4    Miller, K.W.5
  • 74
    • 0028848223 scopus 로고
    • Discrete Site for General Anesthetics on a Postsynaptic Receptor
    • Forman, S.A., Miller, K.W., Yellen, G.A. Discrete Site for General Anesthetics on a Postsynaptic Receptor. Mol. Pharmacol. 48:574-581, 1995.
    • (1995) Mol. Pharmacol. , vol.48 , pp. 574-581
    • Forman, S.A.1    Miller, K.W.2    Yellen, G.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.