메뉴 건너뛰기




Volumn 51, Issue 26, 2012, Pages 5348-5358

An outer membrane protein undergoes enthalpy- and entropy-driven transitions

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVATION ENTHALPIES; ACTIVATION ENTROPIES; CHANNEL GATING; CHANNEL TRANSITION; CURRENT FLUCTUATIONS; CURRENT TRANSITIONS; EQUILIBRIUM FREE ENERGY; FUNCTIONAL TRAITS; HIGH RESOLUTION CRYSTAL STRUCTURE; MEMBRANE PROTEINS; OUTER MEMBRANE; OUTER MEMBRANE PROTEIN; PROTEIN DESIGN; PSEUDOMONAS AERUGINOSA; SINGLE-CHANNEL; SINGLE-MOLECULE; TEMPERATURE DEPENDENT; THERMALLY INDUCED; TRANSMEMBRANES;

EID: 84863535506     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi300332z     Document Type: Article
Times cited : (20)

References (69)
  • 1
    • 0041428149 scopus 로고    scopus 로고
    • The versatile β-barrel membrane protein
    • Wimley, W. C. (2003) The versatile β-barrel membrane protein Curr. Opin. Struct. Biol. 13, 404-411
    • (2003) Curr. Opin. Struct. Biol. , vol.13 , pp. 404-411
    • Wimley, W.C.1
  • 2
    • 0032563173 scopus 로고    scopus 로고
    • Voltage gating is a fundamental feature of porin and toxin β-barrel membrane channels
    • Bainbridge, G., Gokce, I., and Lakey, J. H. (1998) Voltage gating is a fundamental feature of porin and toxin β-barrel membrane channels FEBS Lett. 431, 305-308
    • (1998) FEBS Lett. , vol.431 , pp. 305-308
    • Bainbridge, G.1    Gokce, I.2    Lakey, J.H.3
  • 3
    • 0036968478 scopus 로고    scopus 로고
    • Molecular basis of voltage gating of OmpF porin
    • Robertson, K. M. and Tieleman, D. P. (2002) Molecular basis of voltage gating of OmpF porin Biochem. Cell Biol. 80, 517-523
    • (2002) Biochem. Cell Biol. , vol.80 , pp. 517-523
    • Robertson, K.M.1    Tieleman, D.P.2
  • 5
    • 0032536195 scopus 로고    scopus 로고
    • Voltage-gating of Escherichia coli porin: A cystine-scanning mutagenesis study of loop 3
    • Bainbridge, G., Mobasheri, H., Armstrong, G. A., Lea, E. J. A., and Lakey, J. H. (1998) Voltage-gating of Escherichia coli porin: A cystine-scanning mutagenesis study of loop 3 J. Mol. Biol. 275, 171-176
    • (1998) J. Mol. Biol. , vol.275 , pp. 171-176
    • Bainbridge, G.1    Mobasheri, H.2    Armstrong, G.A.3    Lea, E.J.A.4    Lakey, J.H.5
  • 6
    • 73649132280 scopus 로고    scopus 로고
    • Modulating effects of the plug, helix, and N- and C-terminal domains on channel properties of the PapC usher
    • Mapingire, O. S., Henderson, N. S., Duret, G., Thanassi, D. G., and Delcour, A. H. (2009) Modulating effects of the plug, helix, and N- and C-terminal domains on channel properties of the PapC usher J. Biol. Chem. 284, 36324-36333
    • (2009) J. Biol. Chem. , vol.284 , pp. 36324-36333
    • Mapingire, O.S.1    Henderson, N.S.2    Duret, G.3    Thanassi, D.G.4    Delcour, A.H.5
  • 7
    • 79953129278 scopus 로고    scopus 로고
    • Redesign of a plugged β-barrel membrane protein
    • Mohammad, M. M., Howard, K. R., and Movileanu, L. (2011) Redesign of a plugged β-barrel membrane protein J. Biol. Chem. 286, 8000-8013
    • (2011) J. Biol. Chem. , vol.286 , pp. 8000-8013
    • Mohammad, M.M.1    Howard, K.R.2    Movileanu, L.3
  • 8
    • 0033867375 scopus 로고    scopus 로고
    • Effects of pore mutations and permeant ion concentration on the spontaneous gating activity of OmpC porin
    • Liu, N., Samartzidou, H., Lee, K. W., Briggs, J. M., and Delcour, A. H. (2000) Effects of pore mutations and permeant ion concentration on the spontaneous gating activity of OmpC porin Protein Eng. 13, 491-500
    • (2000) Protein Eng. , vol.13 , pp. 491-500
    • Liu, N.1    Samartzidou, H.2    Lee, K.W.3    Briggs, J.M.4    Delcour, A.H.5
  • 10
    • 77957959675 scopus 로고    scopus 로고
    • Disulfide bond tethering of extracellular loops does not affect the closure of OmpF porin at acidic pH
    • Wager, B., Basle, A., and Delcour, A. H. (2010) Disulfide bond tethering of extracellular loops does not affect the closure of OmpF porin at acidic pH Proteins 78, 2886-2894
    • (2010) Proteins , vol.78 , pp. 2886-2894
    • Wager, B.1    Basle, A.2    Delcour, A.H.3
  • 11
    • 77954340928 scopus 로고    scopus 로고
    • Impact of distant charge reversals within a robust β-barrel protein pore
    • Mohammad, M. M. and Movileanu, L. (2010) Impact of distant charge reversals within a robust β-barrel protein pore J. Phys. Chem. B 114, 8750-8759
    • (2010) J. Phys. Chem. B , vol.114 , pp. 8750-8759
    • Mohammad, M.M.1    Movileanu, L.2
  • 12
    • 77949316155 scopus 로고    scopus 로고
    • PH-induced conformational change of the β-barrel-forming protein OmpG reconstituted into native E. coli lipids
    • Mari, S. A., Koster, S., Bippes, C. A., Yildiz, O., Kuhlbrandt, W., and Muller, D. J. (2010) pH-induced conformational change of the β-barrel-forming protein OmpG reconstituted into native E. coli lipids J. Mol. Biol. 396, 610-616
    • (2010) J. Mol. Biol. , vol.396 , pp. 610-616
    • Mari, S.A.1    Koster, S.2    Bippes, C.A.3    Yildiz, O.4    Kuhlbrandt, W.5    Muller, D.J.6
  • 15
    • 33846434466 scopus 로고    scopus 로고
    • Membrane simulations of OpcA: Gating in the loops?
    • Bond, P. J., Derrick, J. P., and Sansom, M. S. (2007) Membrane simulations of OpcA: Gating in the loops? Biophys. J. 92, L23-L25
    • (2007) Biophys. J. , vol.92
    • Bond, P.J.1    Derrick, J.P.2    Sansom, M.S.3
  • 16
    • 36048936454 scopus 로고    scopus 로고
    • Structure refinement of the OpcA adhesin using molecular dynamics
    • Luan, B., Caffrey, M., and Aksimentiev, A. (2007) Structure refinement of the OpcA adhesin using molecular dynamics Biophys. J. 93, 3058-3069
    • (2007) Biophys. J. , vol.93 , pp. 3058-3069
    • Luan, B.1    Caffrey, M.2    Aksimentiev, A.3
  • 17
    • 33750255413 scopus 로고    scopus 로고
    • Electrostatic couplings in OmpA ion-channel gating suggest a mechanism for pore opening
    • Hong, H., Szabo, G., and Tamm, L. K. (2006) Electrostatic couplings in OmpA ion-channel gating suggest a mechanism for pore opening Nat. Chem. Biol. 2, 627-635
    • (2006) Nat. Chem. Biol. , vol.2 , pp. 627-635
    • Hong, H.1    Szabo, G.2    Tamm, L.K.3
  • 18
    • 79958048597 scopus 로고    scopus 로고
    • Analysis of gating transitions among the three major open states of the OpdK channel
    • Cheneke, B. R., van den Berg, B., and Movileanu, L. (2011) Analysis of gating transitions among the three major open states of the OpdK channel Biochemistry 50, 4987-4997
    • (2011) Biochemistry , vol.50 , pp. 4987-4997
    • Cheneke, B.R.1    Van Den Berg, B.2    Movileanu, L.3
  • 19
    • 33644903806 scopus 로고    scopus 로고
    • Role of the novel OprD family of porins in nutrient uptake in Pseudomonas aeruginosa
    • Tamber, S., Ochs, M. M., and Hancock, R. E. (2006) Role of the novel OprD family of porins in nutrient uptake in Pseudomonas aeruginosa J. Bacteriol. 188, 45-54
    • (2006) J. Bacteriol. , vol.188 , pp. 45-54
    • Tamber, S.1    Ochs, M.M.2    Hancock, R.E.3
  • 20
    • 33646583611 scopus 로고    scopus 로고
    • Porins of the Outer Membrane of Pseudomonas aeruginosa
    • In (Benz, R. Ed.) pp, Wiley-VCH, Weinheim, Germany.
    • Hancock, R. E. W. and Tamber, S. (2004) Porins of the Outer Membrane of Pseudomonas aeruginosa. In Bacterial and Eukaryotic Porins: Structure, Function, Mechanism (Benz, R., Ed.) pp 61-77, Wiley-VCH, Weinheim, Germany.
    • (2004) Bacterial and Eukaryotic Porins: Structure, Function, Mechanism , pp. 61-77
    • Hancock, R.E.W.1    Tamber, S.2
  • 23
    • 84863377489 scopus 로고    scopus 로고
    • OccK Channels from Pseudomonas aeruginosa Exhibit Diverse Single-channel Electrical Signatures, but Conserved Anion Selectivity
    • Liu, J., Eren, E., Vijayaraghavan, J., Cheneke, B. R., Indic, M., van den Berg, B., and Movileanu, L. (2012) OccK Channels from Pseudomonas aeruginosa Exhibit Diverse Single-channel Electrical Signatures, but Conserved Anion Selectivity Biochemistry 51, 2319-2330
    • (2012) Biochemistry , vol.51 , pp. 2319-2330
    • Liu, J.1    Eren, E.2    Vijayaraghavan, J.3    Cheneke, B.R.4    Indic, M.5    Van Den Berg, B.6    Movileanu, L.7
  • 24
    • 46049091548 scopus 로고    scopus 로고
    • Crystal structure of the outer membrane protein OpdK from Pseudomonas aeruginosa
    • Biswas, S., Mohammad, M. M., Movileanu, L., and van den Berg, B. (2008) Crystal structure of the outer membrane protein OpdK from Pseudomonas aeruginosa Structure 16, 1027-1035
    • (2008) Structure , vol.16 , pp. 1027-1035
    • Biswas, S.1    Mohammad, M.M.2    Movileanu, L.3    Van Den Berg, B.4
  • 25
    • 0029018327 scopus 로고
    • Tight regulation, modulation, and high-level expression by vectors containing the arabinose PBAD promotor
    • Guzman, L. M., Belin, D., Carson, M. J., and Beckwith, J. (1995) Tight regulation, modulation, and high-level expression by vectors containing the arabinose PBAD promotor J. Bacteriol. 177, 4121-4130
    • (1995) J. Bacteriol. , vol.177 , pp. 4121-4130
    • Guzman, L.M.1    Belin, D.2    Carson, M.J.3    Beckwith, J.4
  • 26
    • 41149181242 scopus 로고    scopus 로고
    • Controlling a single protein in a nanopore through electrostatic traps
    • Mohammad, M. M., Prakash, S., Matouschek, A., and Movileanu, L. (2008) Controlling a single protein in a nanopore through electrostatic traps J. Am. Chem. Soc. 130, 4081-4088
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 4081-4088
    • Mohammad, M.M.1    Prakash, S.2    Matouschek, A.3    Movileanu, L.4
  • 27
    • 0001774017 scopus 로고
    • Fitting and statistical analysis of single-channel records
    • In (Sackmann, B. N. E. Ed.) 2nd ed. pp, Plenum Press, New York.
    • Colquhoun, D. and Sigworth, F. J. (1995) Fitting and statistical analysis of single-channel records. In Single-channel recording (Sackmann, B. N. E., Ed.) 2nd ed., pp 483-587, Plenum Press, New York.
    • (1995) Single-channel Recording , pp. 483-587
    • Colquhoun, D.1    Sigworth, F.J.2
  • 28
    • 39149121526 scopus 로고    scopus 로고
    • Single-channel recording of ligand-gated ion channels
    • Mortensen, M. and Smart, T. G. (2007) Single-channel recording of ligand-gated ion channels Nat. Protoc. 2, 2826-2841
    • (2007) Nat. Protoc. , vol.2 , pp. 2826-2841
    • Mortensen, M.1    Smart, T.G.2
  • 29
    • 0023549511 scopus 로고
    • Sampling, Log Binning, Fitting, and Plotting Durations of Open and Shut Intervals from Single Channels and the Effects of Noise
    • McManus, O. B., Blatz, A. L., and Magleby, K. L. (1987) Sampling, Log Binning, Fitting, and Plotting Durations of Open and Shut Intervals From Single Channels and the Effects of Noise Pfluegers Arch. 410, 530-553
    • (1987) Pfluegers Arch. , vol.410 , pp. 530-553
    • McManus, O.B.1    Blatz, A.L.2    Magleby, K.L.3
  • 30
    • 0023734971 scopus 로고
    • Kinetic states and modes of single large-conductance calcium-activated potassium channels in cultured rat skeletal-muscle
    • McManus, O. B. and Magleby, K. L. (1988) Kinetic states and modes of single large-conductance calcium-activated potassium channels in cultured rat skeletal-muscle J. Physiol. (Oxford, U.K.) 402, 79-120
    • (1988) J. Physiol. (Oxford, U.K.) , vol.402 , pp. 79-120
    • McManus, O.B.1    Magleby, K.L.2
  • 31
    • 0041843734 scopus 로고    scopus 로고
    • Partitioning of individual flexible polymers into a nanoscopic protein pore
    • Movileanu, L., Cheley, S., and Bayley, H. (2003) Partitioning of individual flexible polymers into a nanoscopic protein pore Biophys. J. 85, 897-910
    • (2003) Biophys. J. , vol.85 , pp. 897-910
    • Movileanu, L.1    Cheley, S.2    Bayley, H.3
  • 32
    • 33845196984 scopus 로고    scopus 로고
    • Temperature-responsive protein pores
    • Jung, Y., Bayley, H., and Movileanu, L. (2006) Temperature-responsive protein pores J. Am. Chem. Soc. 128, 15332-15340
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 15332-15340
    • Jung, Y.1    Bayley, H.2    Movileanu, L.3
  • 33
    • 45849114386 scopus 로고    scopus 로고
    • Excursion of a single polypeptide into a protein pore: Simple physics, but complicated biology
    • Mohammad, M. M. and Movileanu, L. (2008) Excursion of a single polypeptide into a protein pore: Simple physics, but complicated biology Eur. Biophys. J. 37, 913-925
    • (2008) Eur. Biophys. J. , vol.37 , pp. 913-925
    • Mohammad, M.M.1    Movileanu, L.2
  • 36
    • 84860501378 scopus 로고    scopus 로고
    • Protein Sensing with Engineered Protein Nanopores
    • In (Graceva, M. E. Ed.) Vol. pp, Springer, New York.
    • Mohammad, M. M. and Movileanu, L. (2012) Protein Sensing with Engineered Protein Nanopores. In Nanopore-Based Technology: Methods in Molecular Biology Series (Graceva, M. E., Ed.) Vol. 870, pp 21-37, Springer, New York.
    • (2012) Nanopore-Based Technology: Methods in Molecular Biology Series , vol.870 , pp. 21-37
    • Mohammad, M.M.1    Movileanu, L.2
  • 37
    • 0025255092 scopus 로고
    • Buffers: Principles and practice
    • Stoll, V. S. and Blanchard, J. S. (1990) Buffers: Principles and practice Methods Enzymol. 182, 24-38
    • (1990) Methods Enzymol. , vol.182 , pp. 24-38
    • Stoll, V.S.1    Blanchard, J.S.2
  • 39
    • 16244372752 scopus 로고    scopus 로고
    • Single Protein Pores Containing Molecular Adapters at High Temperatures
    • Kang, X. F., Gu, L. Q., Cheley, S., and Bayley, H. (2005) Single Protein Pores Containing Molecular Adapters at High Temperatures Angew. Chem., Int. Ed. 44, 1495-1499
    • (2005) Angew. Chem., Int. Ed. , vol.44 , pp. 1495-1499
    • Kang, X.F.1    Gu, L.Q.2    Cheley, S.3    Bayley, H.4
  • 40
    • 71549118233 scopus 로고    scopus 로고
    • Buffers: Principles and practice
    • Stoll, V. S. and Blanchard, J. S. (2009) Buffers: Principles and practice Methods Enzymol. 463, 43-56
    • (2009) Methods Enzymol. , vol.463 , pp. 43-56
    • Stoll, V.S.1    Blanchard, J.S.2
  • 42
    • 0018878793 scopus 로고
    • Rate theory calculation of gramicidin single-channel currents using NMR-derived rate constants
    • Urry, D. W., Venkatachalam, C. M., Spisni, A., Lauger, P., and Khaled, M. A. (1980) Rate theory calculation of gramicidin single-channel currents using NMR-derived rate constants Proc. Natl. Acad. Sci. U.S.A. 77, 2028-2032
    • (1980) Proc. Natl. Acad. Sci. U.S.A. , vol.77 , pp. 2028-2032
    • Urry, D.W.1    Venkatachalam, C.M.2    Spisni, A.3    Lauger, P.4    Khaled, M.A.5
  • 43
    • 0024409669 scopus 로고
    • Activation kinetics of single high-threshold calcium channels in the membrane of sensory neurons from mouse embryos
    • Kostyuk, P. G., Shuba, Y., and Teslenko, V. I. (1989) Activation kinetics of single high-threshold calcium channels in the membrane of sensory neurons from mouse embryos J. Membr. Biol. 110, 29-38
    • (1989) J. Membr. Biol. , vol.110 , pp. 29-38
    • Kostyuk, P.G.1    Shuba, Y.2    Teslenko, V.I.3
  • 44
    • 10544228592 scopus 로고    scopus 로고
    • Concepts of single-channel analysis: Inferring function from fluctuations
    • In (Ashley, R. H. Ed.) 2nd ed. pp, Oxford University Press, Oxford, U.K.
    • Moss, G. W. J. and Moczydlowski, E. (2002) Concepts of single-channel analysis: Inferring function from fluctuations. In Ion Channels: A Practical Approach (Ashley, R. H., Ed.) 2nd ed., pp 69-112, Oxford University Press, Oxford, U.K.
    • (2002) Ion Channels: A Practical Approach , pp. 69-112
    • Moss, G.W.J.1    Moczydlowski, E.2
  • 46
    • 78149459196 scopus 로고    scopus 로고
    • Facilitated translocation of polypeptides through a single nanopore
    • Bikwemu, R., Wolfe, A. J., Xing, X., and Movileanu, L. (2010) Facilitated translocation of polypeptides through a single nanopore J. Phys.: Condens. Matter 22, 454117
    • (2010) J. Phys.: Condens. Matter , vol.22 , pp. 454117
    • Bikwemu, R.1    Wolfe, A.J.2    Xing, X.3    Movileanu, L.4
  • 47
    • 0016927165 scopus 로고
    • Diffusion frequency factors in some simple examples of transition-state rate theory
    • Hill, T. L. (1976) Diffusion frequency factors in some simple examples of transition-state rate theory Proc. Natl. Acad. Sci. U.S.A. 73, 679-683
    • (1976) Proc. Natl. Acad. Sci. U.S.A. , vol.73 , pp. 679-683
    • Hill, T.L.1
  • 48
    • 0001630589 scopus 로고
    • Characterization of thermal-isomerization at the single-molecule level
    • Jaikaran, D. C. J. and Woolley, G. A. (1995) Characterization of thermal-isomerization at the single-molecule level J. Phys. Chem. 99, 13352-13355
    • (1995) J. Phys. Chem. , vol.99 , pp. 13352-13355
    • Jaikaran, D.C.J.1    Woolley, G.A.2
  • 49
    • 0035818604 scopus 로고    scopus 로고
    • Kinetics of duplex formation for individual DNA strands within a single protein nanopore
    • Howorka, S., Movileanu, L., Braha, O., and Bayley, H. (2001) Kinetics of duplex formation for individual DNA strands within a single protein nanopore Proc. Natl. Acad. Sci. U.S.A. 98, 12996-13001
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 12996-13001
    • Howorka, S.1    Movileanu, L.2    Braha, O.3    Bayley, H.4
  • 50
    • 0033210507 scopus 로고    scopus 로고
    • Graphic representation of the results of kinetic analyses
    • Andersen, O. S. (1999) Graphic representation of the results of kinetic analyses J. Gen. Physiol. 114, 589-590
    • (1999) J. Gen. Physiol. , vol.114 , pp. 589-590
    • Andersen, O.S.1
  • 51
    • 0015788893 scopus 로고
    • Ion transport through pores: A rate-theory analysis
    • Lauger, P. (1973) Ion transport through pores: A rate-theory analysis Biochim. Biophys. Acta 311, 423-441
    • (1973) Biochim. Biophys. Acta , vol.311 , pp. 423-441
    • Lauger, P.1
  • 52
    • 0032849370 scopus 로고    scopus 로고
    • Ion permeation and chemical kinetics
    • Jordan, P. C. (1999) Ion permeation and chemical kinetics J. Gen. Physiol. 114, 601-603
    • (1999) J. Gen. Physiol. , vol.114 , pp. 601-603
    • Jordan, P.C.1
  • 54
    • 33750499982 scopus 로고    scopus 로고
    • Thermodynamics of CFTR channel gating: A spreading conformational change initiates an irreversible gating cycle
    • Csanady, L., Nairn, A. C., and Gadsby, D. C. (2006) Thermodynamics of CFTR channel gating: A spreading conformational change initiates an irreversible gating cycle J. Gen. Physiol. 128, 523-533
    • (2006) J. Gen. Physiol. , vol.128 , pp. 523-533
    • Csanady, L.1    Nairn, A.C.2    Gadsby, D.C.3
  • 55
    • 55549135721 scopus 로고    scopus 로고
    • Thermodynamics of activation gating in olfactory-type cyclic nucleotide-gated (CNGA2) channels
    • Nache, V., Kusch, J., Biskup, C., Schulz, E., Zimmer, T., Hagen, V., and Benndorf, K. (2008) Thermodynamics of activation gating in olfactory-type cyclic nucleotide-gated (CNGA2) channels Biophys. J. 95, 2750-2758
    • (2008) Biophys. J. , vol.95 , pp. 2750-2758
    • Nache, V.1    Kusch, J.2    Biskup, C.3    Schulz, E.4    Zimmer, T.5    Hagen, V.6    Benndorf, K.7
  • 56
    • 0347193736 scopus 로고
    • Reaction-Rate Theory: 50 Years after Kramers
    • Hanggi, P., Talkner, P., and Borkovec, M. (1990) Reaction-Rate Theory: 50 Years After Kramers Rev. Mod. Phys. 62, 251-341
    • (1990) Rev. Mod. Phys. , vol.62 , pp. 251-341
    • Hanggi, P.1    Talkner, P.2    Borkovec, M.3
  • 57
    • 0028981210 scopus 로고
    • Negative activation enthalpies in the kinetics of protein folding
    • Oliveberg, M., Tan, Y. J., and Fersht, A. R. (1995) Negative activation enthalpies in the kinetics of protein folding Proc. Natl. Acad. Sci. U.S.A. 92, 8926-8929
    • (1995) Proc. Natl. Acad. Sci. U.S.A. , vol.92 , pp. 8926-8929
    • Oliveberg, M.1    Tan, Y.J.2    Fersht, A.R.3
  • 58
    • 0036712053 scopus 로고    scopus 로고
    • Determination of base and backbone contributions to the thermodynamics of premelting and melting transitions in B DNA
    • Movileanu, L., Benevides, J. M., and Thomas, G. J. (2002) Determination of base and backbone contributions to the thermodynamics of premelting and melting transitions in B DNA Nucleic Acids Res. 30, 3767-3777
    • (2002) Nucleic Acids Res. , vol.30 , pp. 3767-3777
    • Movileanu, L.1    Benevides, J.M.2    Thomas, G.J.3
  • 59
    • 79951831689 scopus 로고    scopus 로고
    • Mapping heat exchange in an allosteric protein
    • Gupta, S. and Auerbach, A. (2011) Mapping heat exchange in an allosteric protein Biophys. J. 100, 904-911
    • (2011) Biophys. J. , vol.100 , pp. 904-911
    • Gupta, S.1    Auerbach, A.2
  • 61
    • 77952273078 scopus 로고    scopus 로고
    • Comparing the temperature-dependent conductance of the two structurally similar E. coli porins OmpC and OmpF
    • Biro, I., Pezeshki, S., Weingart, H., Winterhalter, M., and Kleinekathofer, U. (2010) Comparing the temperature-dependent conductance of the two structurally similar E. coli porins OmpC and OmpF Biophys. J. 98, 1830-1839
    • (2010) Biophys. J. , vol.98 , pp. 1830-1839
    • Biro, I.1    Pezeshki, S.2    Weingart, H.3    Winterhalter, M.4    Kleinekathofer, U.5
  • 63
    • 77955444568 scopus 로고    scopus 로고
    • Thermal unfolding kinetics of ubiquitin in the microsecond-to-second time range probed by Tyr-59 fluorescence
    • Noronha, M., Gerbelova, H., Faria, T. Q., Lund, D. N., Smith, D. A., Santos, H., and Macanita, A. L. (2010) Thermal unfolding kinetics of ubiquitin in the microsecond-to-second time range probed by Tyr-59 fluorescence J. Phys. Chem. B 114, 9912-9919
    • (2010) J. Phys. Chem. B , vol.114 , pp. 9912-9919
    • Noronha, M.1    Gerbelova, H.2    Faria, T.Q.3    Lund, D.N.4    Smith, D.A.5    Santos, H.6    MacAnita, A.L.7
  • 64
    • 0242385383 scopus 로고    scopus 로고
    • Thermodynamics of heat activation of single capsaicin ion channels VR1
    • Liu, B., Hui, K., and Qin, F. (2003) Thermodynamics of heat activation of single capsaicin ion channels VR1 Biophys. J. 85, 2988-3006
    • (2003) Biophys. J. , vol.85 , pp. 2988-3006
    • Liu, B.1    Hui, K.2    Qin, F.3
  • 65
    • 67650351332 scopus 로고    scopus 로고
    • Rapid temperature jump by infrared diode laser irradiation for patch-clamp studies
    • Yao, J., Liu, B., and Qin, F. (2009) Rapid temperature jump by infrared diode laser irradiation for patch-clamp studies Biophys. J. 96, 3611-3619
    • (2009) Biophys. J. , vol.96 , pp. 3611-3619
    • Yao, J.1    Liu, B.2    Qin, F.3
  • 66
    • 79951834831 scopus 로고    scopus 로고
    • Temperature dependence of acetylcholine receptor channels activated by different agonists
    • Gupta, S. and Auerbach, A. (2011) Temperature dependence of acetylcholine receptor channels activated by different agonists Biophys. J. 100, 895-903
    • (2011) Biophys. J. , vol.100 , pp. 895-903
    • Gupta, S.1    Auerbach, A.2
  • 67
    • 0029395478 scopus 로고
    • Win some, lose some: Enthalpy-entropy compensation in weak intermolecular interactions
    • Dunitz, J. D. (1995) Win some, lose some: Enthalpy-entropy compensation in weak intermolecular interactions Chem. Biol. 2, 709-712
    • (1995) Chem. Biol. , vol.2 , pp. 709-712
    • Dunitz, J.D.1
  • 68
    • 0026752083 scopus 로고
    • + channels in the squid giant axon. Voltage and temperature effects
    • + channels in the squid giant axon. Voltage and temperature effects Biophys. J. 61, 1332-1352
    • (1992) Biophys. J. , vol.61 , pp. 1332-1352
    • Correa, A.M.1    Bezanilla, F.2    Latorre, R.3
  • 69
    • 36148943499 scopus 로고    scopus 로고
    • Catalyzing the translocation of polypeptides through attractive interactions
    • Wolfe, A. J., Mohammad, M. M., Cheley, S., Bayley, H., and Movileanu, L. (2007) Catalyzing the translocation of polypeptides through attractive interactions J. Am. Chem. Soc. 129, 14034-14041
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 14034-14041
    • Wolfe, A.J.1    Mohammad, M.M.2    Cheley, S.3    Bayley, H.4    Movileanu, L.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.