메뉴 건너뛰기




Volumn 8590, Issue , 2013, Pages

Subunit rotation in single FRET-labeled F1-ATPase hold in solution by an anti-Brownian electrokinetic trap

Author keywords

ABELtrap; F1 ATPase; Hidden Markov Model; single molecule FRET; subunit rotation

Indexed keywords

ABELTRAP; ELECTROKINETIC TRAP; HYDROLYZING ENZYMES; MONTE CARLO SIMULATIONS; RESONANCE ENERGY TRANSFER; SIGNAL-TO-BACKGROUND RATIO; SINGLE-MOLECULE FRETS; SUBUNIT ROTATION;

EID: 84878087658     PISSN: 16057422     EISSN: None     Source Type: Conference Proceeding    
DOI: 10.1117/12.2002955     Document Type: Conference Paper
Times cited : (8)

References (81)
  • 1
    • 0031588861 scopus 로고    scopus 로고
    • Catalytic mechanism of F1-ATPase
    • Weber, J., and Senior, A.E., "Catalytic mechanism of F1-ATPase," Biochim Biophys Acta 1319, 19-58 (1997).
    • (1997) Biochim Biophys Acta , vol.1319 , pp. 19-58
    • Weber, J.1    Senior, A.E.2
  • 2
    • 79958858245 scopus 로고    scopus 로고
    • Structure of the ATP synthase catalytic complex (F(1)) from Escherichia coli in an autoinhibited conformation
    • Cingolani, G., and Duncan, T.M., "Structure of the ATP synthase catalytic complex (F(1)) from Escherichia coli in an autoinhibited conformation," Nat Struct Mol Biol 18, 701-707 (2011).
    • (2011) Nat Struct Mol Biol , vol.18 , pp. 701-707
    • Cingolani, G.1    Duncan, T.M.2
  • 3
    • 84867254749 scopus 로고    scopus 로고
    • Improved crystallization of Escherichia coli ATP synthase catalytic complex (F1) by introducing a phosphomimetic mutation in subunit epsilon
    • Roy, A., Hutcheon, M.L., Duncan, T.M., and Cingolani, G., "Improved crystallization of Escherichia coli ATP synthase catalytic complex (F1) by introducing a phosphomimetic mutation in subunit epsilon," Acta Crystallogr Sect F Struct Biol Cryst Commun 68, 1229-1233 (2012).
    • (2012) Acta Crystallogr Sect F Struct Biol Cryst Commun , vol.68 , pp. 1229-1233
    • Roy, A.1    Hutcheon, M.L.2    Duncan, T.M.3    Cingolani, G.4
  • 5
    • 0030592156 scopus 로고    scopus 로고
    • ATP hydrolysis by membrane-bound Escherichia coli F0F1 causes rotation of the gamma subunit relative to the beta subunits
    • Zhou, Y., Duncan, T.M., Bulygin, V.V., Hutcheon, M.L., and Cross, R.L., "ATP hydrolysis by membrane-bound Escherichia coli F0F1 causes rotation of the gamma subunit relative to the beta subunits," Biochim Biophys Acta 1275, 96- 100 (1996).
    • (1996) Biochim Biophys Acta , vol.1275 , pp. 96-100
    • Zhou, Y.1    Duncan, T.M.2    Bulygin, V.V.3    Hutcheon, M.L.4    Cross, R.L.5
  • 6
    • 0032947857 scopus 로고    scopus 로고
    • Transient accumulation of elastic energy in proton translocating ATP synthase
    • Cherepanov, D.A., Mulkidjanian, A.Y., and Junge, W., "Transient accumulation of elastic energy in proton translocating ATP synthase," FEBS Lett 449, 1-6 (1999).
    • (1999) FEBS Lett , vol.449 , pp. 1-6
    • Cherepanov, D.A.1    Mulkidjanian, A.Y.2    Junge, W.3
  • 9
    • 66249132322 scopus 로고    scopus 로고
    • Torque generation and elastic power transmission in the rotary FOF1-ATPase
    • Junge, W., Sielaff, H., and Engelbrecht, S., "Torque generation and elastic power transmission in the rotary FOF1-ATPase," Nature 459, 364-370 (2009).
    • (2009) Nature , vol.459 , pp. 364-370
    • Junge, W.1    Sielaff, H.2    Engelbrecht, S.3
  • 10
    • 79957819196 scopus 로고    scopus 로고
    • Rotation and structure of FoF1-ATP synthase
    • Okuno, D., Iino, R., and Noji, H., "Rotation and structure of FoF1-ATP synthase," J Biochem 149, 655-664 (2011).
    • (2011) J Biochem , vol.149 , pp. 655-664
    • Okuno, D.1    Iino, R.2    Noji, H.3
  • 11
    • 0035912221 scopus 로고    scopus 로고
    • Resolution of distinct rotational substeps by submillisecond kinetic analysis of F1-ATPase
    • Yasuda, R., Noji, H., Yoshida, M., Kinosita, K., Jr., and Itoh, H., "Resolution of distinct rotational substeps by submillisecond kinetic analysis of F1-ATPase," Nature 410, 898-904 (2001).
    • (2001) Nature , vol.410 , pp. 898-904
    • Yasuda, R.1    Noji, H.2    Yoshida, M.3    Kinosita Jr., K.4    Itoh, H.5
  • 13
    • 33645218407 scopus 로고    scopus 로고
    • Stochastic high-speed rotation of Escherichia coli ATP synthase F1 sector: The epsilon subunit-sensitive rotation
    • Nakanishi-Matsui, M., Kashiwagi, S., Hosokawa, H., Cipriano, D.J., Dunn, S.D., Wada, Y., and Futai, M., "Stochastic high-speed rotation of Escherichia coli ATP synthase F1 sector: the epsilon subunit-sensitive rotation," J Biol Chem 281, 4126-4131 (2006).
    • (2006) J Biol Chem , vol.281 , pp. 4126-4131
    • Nakanishi-Matsui, M.1    Kashiwagi, S.2    Hosokawa, H.3    Cipriano, D.J.4    Dunn, S.D.5    Wada, Y.6    Futai, M.7
  • 14
    • 0030611634 scopus 로고    scopus 로고
    • Crystal structure of the epsilon subunit of the proton-translocating ATP synthase from Escherichia coli
    • Uhlin, U., Cox, G.B., and Guss, J.M., "Crystal structure of the epsilon subunit of the proton-translocating ATP synthase from Escherichia coli," Structure 5, 1219-1230 (1997).
    • (1997) Structure , vol.5 , pp. 1219-1230
    • Uhlin, U.1    Cox, G.B.2    Guss, J.M.3
  • 15
    • 0032500380 scopus 로고    scopus 로고
    • Solution structure of the epsilon subunit of the F1-ATPase from Escherichia coli and interactions of this subunit with beta subunits in the complex
    • Wilkens, S., and Capaldi, R.A., "Solution structure of the epsilon subunit of the F1-ATPase from Escherichia coli and interactions of this subunit with beta subunits in the complex," J Biol Chem 273, 26645-26651 (1998).
    • (1998) J Biol Chem , vol.273 , pp. 26645-26651
    • Wilkens, S.1    Capaldi, R.A.2
  • 16
    • 0033766435 scopus 로고    scopus 로고
    • The structure of the central stalk in bovine F(1)-ATPase at 2.4 A resolution
    • Gibbons, C., Montgomery, M.G., Leslie, A.G., and Walker, J.E., "The structure of the central stalk in bovine F(1)-ATPase at 2.4 A resolution," Nat Struct Biol 7, 1055-1061 (2000).
    • (2000) Nat Struct Biol , vol.7 , pp. 1055-1061
    • Gibbons, C.1    Montgomery, M.G.2    Leslie, A.G.3    Walker, J.E.4
  • 17
    • 0035861587 scopus 로고    scopus 로고
    • The conformation of the epsilon- and gamma-subunits within the Escherichia coli F(1) ATPase
    • Hausrath, A.C., Capaldi, R.A., and Matthews, B.W., "The conformation of the epsilon- and gamma-subunits within the Escherichia coli F(1) ATPase," J Biol Chem 276, 47227-47232 (2001).
    • (2001) J Biol Chem , vol.276 , pp. 47227-47232
    • Hausrath, A.C.1    Capaldi, R.A.2    Matthews, B.W.3
  • 18
    • 77951214694 scopus 로고    scopus 로고
    • Activation and stiffness of the inhibited states of F1-ATPase probed by single-molecule manipulation
    • Saita, E., Iino, R., Suzuki, T., Feniouk, B.A., Kinosita, K., Jr., and Yoshida, M., "Activation and stiffness of the inhibited states of F1-ATPase probed by single-molecule manipulation," J Biol Chem 285, 11411-11417 (2010).
    • (2010) J Biol Chem , vol.285 , pp. 11411-11417
    • Saita, E.1    Iino, R.2    Suzuki, T.3    Feniouk, B.A.4    Kinosita Jr., K.5    Yoshida, M.6
  • 19
    • 67650555415 scopus 로고    scopus 로고
    • Mechanism of inhibition by C-terminal alpha-helices of the epsilon subunit of Escherichia coli FoF1-ATP synthase
    • Iino, R., Hasegawa, R., Tabata, K.V., and Noji, H., "Mechanism of inhibition by C-terminal alpha-helices of the epsilon subunit of Escherichia coli FoF1-ATP synthase," J Biol Chem 284, 17457-17464 (2009).
    • (2009) J Biol Chem , vol.284 , pp. 17457-17464
    • Iino, R.1    Hasegawa, R.2    Tabata, K.V.3    Noji, H.4
  • 20
    • 0025323480 scopus 로고
    • Activation of Escherichia coli F1-ATPase by lauryldimethylamine oxide and ethylene glycol: Relationship of ATPase activity to the interaction of the epsilon and beta subunits
    • Dunn, S.D., Tozer, R.G., and Zadorozny, V.D., "Activation of Escherichia coli F1-ATPase by lauryldimethylamine oxide and ethylene glycol: relationship of ATPase activity to the interaction of the epsilon and beta subunits," Biochemistry 29, 4335-4340 (1990).
    • (1990) Biochemistry , vol.29 , pp. 4335-4340
    • Dunn, S.D.1    Tozer, R.G.2    Zadorozny, V.D.3
  • 21
    • 0033623349 scopus 로고    scopus 로고
    • Structure of the gamma-epsilon complex of ATP synthase
    • Rodgers, A.J., and Wilce, M.C., "Structure of the gamma-epsilon complex of ATP synthase," Nat Struct Biol 7, 1051-1054 (2000).
    • (2000) Nat Struct Biol , vol.7 , pp. 1051-1054
    • Rodgers, A.J.1    Wilce, M.C.2
  • 22
    • 0032561257 scopus 로고    scopus 로고
    • Conformational changes of the H+-ATPase from Escherichia coli upon nucleotide binding detected by single molecule fluorescence
    • Borsch, M., Turina, P., Eggeling, C., Fries, J.R., Seidel, C.A., Labahn, A., and Graber, P., "Conformational changes of the H+-ATPase from Escherichia coli upon nucleotide binding detected by single molecule fluorescence," FEBS Lett 437, 251-254 (1998).
    • (1998) FEBS Lett , vol.437 , pp. 251-254
    • Borsch, M.1    Turina, P.2    Eggeling, C.3    Fries, J.R.4    Seidel, C.A.5    Labahn, A.6    Graber, P.7
  • 23
    • 0037063327 scopus 로고    scopus 로고
    • Stepwise rotation of the gamma-subunit of EF(0)F(1)-ATP synthase observed by intramolecular single-molecule fluorescence resonance energy transfer
    • Borsch, M., Diez, M., Zimmermann, B., Reuter, R., and Graber, P., "Stepwise rotation of the gamma-subunit of EF(0)F(1)-ATP synthase observed by intramolecular single-molecule fluorescence resonance energy transfer," FEBS Lett 527, 147-152 (2002).
    • (2002) FEBS Lett , vol.527 , pp. 147-152
    • Borsch, M.1    Diez, M.2    Zimmermann, B.3    Reuter, R.4    Graber, P.5
  • 24
    • 0242411076 scopus 로고    scopus 로고
    • Stepwise rotation of the gamma-subunit of EFoF1-ATP synthase during ATP synthesis: A single-molecule FRET approach
    • Borsch, M., Diez, M., Zimmermann, B., Trost, M., Steigmiller, S., and Graber, P., "Stepwise rotation of the gamma-subunit of EFoF1-ATP synthase during ATP synthesis: a single-molecule FRET approach," Proc. SPIE 4962, 11-21 (2003).
    • (2003) Proc. SPIE , vol.4962 , pp. 11-21
    • Borsch, M.1    Diez, M.2    Zimmermann, B.3    Trost, M.4    Steigmiller, S.5    Graber, P.6
  • 26
    • 0942301383 scopus 로고    scopus 로고
    • Binding of the b-subunit in the ATP synthase from Escherichia coli
    • Diez, M., Borsch, M., Zimmermann, B., Turina, P., Dunn, S.D., and Graber, P., "Binding of the b-subunit in the ATP synthase from Escherichia coli," Biochemistry 43, 1054-1064 (2004).
    • (2004) Biochemistry , vol.43 , pp. 1054-1064
    • Diez, M.1    Borsch, M.2    Zimmermann, B.3    Turina, P.4    Dunn, S.D.5    Graber, P.6
  • 27
    • 21844466207 scopus 로고    scopus 로고
    • Movements of the epsilon-subunit during catalysis and activation in single membrane-bound H(+)-ATP synthase
    • Zimmermann, B., Diez, M., Zarrabi, N., Graber, P., and Borsch, M., "Movements of the epsilon-subunit during catalysis and activation in single membrane-bound H(+)-ATP synthase," Embo J 24, 2053-2063 (2005).
    • (2005) Embo J , vol.24 , pp. 2053-2063
    • Zimmermann, B.1    Diez, M.2    Zarrabi, N.3    Graber, P.4    Borsch, M.5
  • 28
    • 21844472504 scopus 로고    scopus 로고
    • Asymmetry of rotational catalysis of single membrane-bound F0F1-ATP synthase
    • Zarrabi, N., Zimmermann, B., Diez, M., Graber, P., Wrachtrup, J., and Borsch, M., "Asymmetry of rotational catalysis of single membrane-bound F0F1-ATP synthase," Proc. SPIE 5699, 175-188 (2005).
    • (2005) Proc. SPIE , vol.5699 , pp. 175-188
    • Zarrabi, N.1    Zimmermann, B.2    Diez, M.3    Graber, P.4    Wrachtrup, J.5    Borsch, M.6
  • 29
    • 33745606026 scopus 로고    scopus 로고
    • Subunit movements in membrane-integrated EF0F1 during ATP synthesis detected by single-molecule spectroscopy
    • Zimmermann, B., Diez, M., Borsch, M., and Graber, P., "Subunit movements in membrane-integrated EF0F1 during ATP synthesis detected by single-molecule spectroscopy," Biochim Biophys Acta 1757, 311-319 (2006).
    • (2006) Biochim Biophys Acta , vol.1757 , pp. 311-319
    • Zimmermann, B.1    Diez, M.2    Borsch, M.3    Graber, P.4
  • 31
    • 34247341351 scopus 로고    scopus 로고
    • Detecting substeps in the rotary motors of FoF1-ATP synthase by Hidden Markov Models
    • Zarrabi, N., Duser, M.G., Reuter, R., Dunn, S.D., Wrachtrup, J., and Borsch, M., "Detecting substeps in the rotary motors of FoF1-ATP synthase by Hidden Markov Models," Proc. SPIE 6444, 64440E (2007).
    • (2007) Proc. SPIE , vol.6444
    • Zarrabi, N.1    Duser, M.G.2    Reuter, R.3    Dunn, S.D.4    Wrachtrup, J.5    Borsch, M.6
  • 32
    • 25844473421 scopus 로고    scopus 로고
    • Both rotor and stator subunits are necessary for efficient binding of F1 to F0 in functionally assembled Escherichia coli ATP synthase
    • Krebstakies, T., Zimmermann, B., Graber, P., Altendorf, K., Borsch, M., and Greie, J.C., "Both rotor and stator subunits are necessary for efficient binding of F1 to F0 in functionally assembled Escherichia coli ATP synthase," J Biol Chem 280, 33338-33345 (2005).
    • (2005) J Biol Chem , vol.280 , pp. 33338-33345
    • Krebstakies, T.1    Zimmermann, B.2    Graber, P.3    Altendorf, K.4    Borsch, M.5    Greie, J.C.6
  • 33
    • 57749093478 scopus 로고    scopus 로고
    • The proton-translocating a subunit of F0F1-ATP synthase is allocated asymmetrically to the peripheral stalk
    • Duser, M.G., Bi, Y., Zarrabi, N., Dunn, S.D., and Borsch, M., "The proton-translocating a subunit of F0F1-ATP synthase is allocated asymmetrically to the peripheral stalk," J Biol Chem 283, 33602-33610 (2008).
    • (2008) J Biol Chem , vol.283 , pp. 33602-33610
    • Duser, M.G.1    Bi, Y.2    Zarrabi, N.3    Dunn, S.D.4    Borsch, M.5
  • 34
  • 35
    • 66849142394 scopus 로고    scopus 로고
    • Simultaneous monitoring of the two coupled motors of a single FoF1-ATP synthase by three-color FRET using duty cycle-optimized triple-ALEX
    • Zarrabi, N., Ernst, S., Duser, M.G., Golovina-Leiker, A., Becker, W., Erdmann, R., Dunn, S.D., and Borsch, M., "Simultaneous monitoring of the two coupled motors of a single FoF1-ATP synthase by three-color FRET using duty cycle-optimized triple-ALEX," Proc. SPIE 7185, 718505 (2009).
    • (2009) Proc. SPIE , vol.7185 , pp. 718505
    • Zarrabi, N.1    Ernst, S.2    Duser, M.G.3    Golovina-Leiker, A.4    Becker, W.5    Erdmann, R.6    Dunn, S.D.7    Borsch, M.8
  • 36
    • 84861450901 scopus 로고    scopus 로고
    • Three-color Förster resonance energy transfer within single FoF1-ATP synthases: Monitoring elastic deformations of the rotary double motor in real time
    • Ernst, S., Duser, M.G., Zarrabi, N., and Borsch, M., "Three-color Förster resonance energy transfer within single FoF1-ATP synthases: monitoring elastic deformations of the rotary double motor in real time," J Biomed Opt 17, 011004 (2012).
    • (2012) J Biomed Opt , vol.17 , pp. 011004
    • Ernst, S.1    Duser, M.G.2    Zarrabi, N.3    Borsch, M.4
  • 37
    • 84864646860 scopus 로고    scopus 로고
    • Elastic deformations of the rotary double motor of single FoF1-ATP synthases detected in real time by Förster resonance energy transfer
    • Ernst, S., Duser, M.G., Zarrabi, N., Dunn, S.D., and Borsch, M., "Elastic deformations of the rotary double motor of single FoF1-ATP synthases detected in real time by Förster resonance energy transfer," Biochimica et Biophysica Acta (BBA) - Bioenergetics 1817, 1722-1731 (2012).
    • (2012) Biochimica et Biophysica Acta (BBA) - Bioenergetics , vol.1817 , pp. 1722-1731
    • Ernst, S.1    Duser, M.G.2    Zarrabi, N.3    Dunn, S.D.4    Borsch, M.5
  • 38
    • 20444460846 scopus 로고    scopus 로고
    • Distances between the b-subunits in the tether domain of F(0)F(1)- ATP synthase from E. coli
    • Steigmiller, S., Borsch, M., Graber, P., and Huber, M., "Distances between the b-subunits in the tether domain of F(0)F(1)- ATP synthase from E. coli," Biochim Biophys Acta 1708, 143-153 (2005).
    • (2005) Biochim Biophys Acta , vol.1708 , pp. 143-153
    • Steigmiller, S.1    Borsch, M.2    Graber, P.3    Huber, M.4
  • 39
    • 2042523545 scopus 로고    scopus 로고
    • Binding of single nucleotides to H+-ATP synthases observed by fluorescence resonance energy transfer
    • Steigmiller, S., Zimmermann, B., Diez, M., Borsch, M., and Graber, P., "Binding of single nucleotides to H+-ATP synthases observed by fluorescence resonance energy transfer," Bioelectrochemistry 63, 79-85 (2004).
    • (2004) Bioelectrochemistry , vol.63 , pp. 79-85
    • Steigmiller, S.1    Zimmermann, B.2    Diez, M.3    Borsch, M.4    Graber, P.5
  • 40
    • 0037163855 scopus 로고    scopus 로고
    • Binding affinities and protein ligand complex geometries of nucleotides at the F(1) part of the mitochondrial ATP synthase obtained by ligand docking calculations
    • Steinbrecher, T., Hucke, O., Steigmiller, S., Borsch, M., and Labahn, A., "Binding affinities and protein ligand complex geometries of nucleotides at the F(1) part of the mitochondrial ATP synthase obtained by ligand docking calculations," FEBS Lett 530, 99-103 (2002).
    • (2002) FEBS Lett , vol.530 , pp. 99-103
    • Steinbrecher, T.1    Hucke, O.2    Steigmiller, S.3    Borsch, M.4    Labahn, A.5
  • 41
    • 0035868171 scopus 로고    scopus 로고
    • In situ temperature measurements via ruby R lines of sapphire substrate based InGaN light emitting diodes during operation
    • Winnewisser, C., Schneider, J., Borsch, M., and Rotter, H.W., "In situ temperature measurements via ruby R lines of sapphire substrate based InGaN light emitting diodes during operation," Journal of Applied Physics 89, 3091-3094 (2001).
    • (2001) Journal of Applied Physics , vol.89 , pp. 3091-3094
    • Winnewisser, C.1    Schneider, J.2    Borsch, M.3    Rotter, H.W.4
  • 42
    • 3042785832 scopus 로고    scopus 로고
    • Real-time pH microscopy down to the molecular level by combined scanning electrochemical microscopy/single-molecule fluorescence spectroscopy
    • Boldt, F.M., Heinze, J., Diez, M., Petersen, J., and Borsch, M., "Real-time pH microscopy down to the molecular level by combined scanning electrochemical microscopy/single-molecule fluorescence spectroscopy," Anal Chem 76, 3473-3481 (2004).
    • (2004) Anal Chem , vol.76 , pp. 3473-3481
    • Boldt, F.M.1    Heinze, J.2    Diez, M.3    Petersen, J.4    Borsch, M.5
  • 43
    • 78651378839 scopus 로고    scopus 로고
    • Single-molecule fluorescence resonance energy transfer techniques on rotary ATP synthases
    • Borsch, M., "Single-molecule fluorescence resonance energy transfer techniques on rotary ATP synthases," Biological Chemistry 392, 135-142 (2011).
    • (2011) Biological Chemistry , vol.392 , pp. 135-142
    • Borsch, M.1
  • 44
    • 79951961078 scopus 로고    scopus 로고
    • Improving FRET-based monitoring of single chemomechanical rotary motors at work
    • Borsch, M., and Wrachtrup, J., "Improving FRET-based monitoring of single chemomechanical rotary motors at work," Chemphyschem 12, 542-553 (2011).
    • (2011) Chemphyschem , vol.12 , pp. 542-553
    • Borsch, M.1    Wrachtrup, J.2
  • 45
    • 53849107484 scopus 로고    scopus 로고
    • Quantum dots for single-pair fluorescence resonance energy transfer in membrane- integrated EFoF1
    • Galvez, E., Duser, M., Borsch, M., Wrachtrup, J., and Graber, P., "Quantum dots for single-pair fluorescence resonance energy transfer in membrane- integrated EFoF1," Biochem Soc Trans 36, 1017-1021 (2008).
    • (2008) Biochem Soc Trans , vol.36 , pp. 1017-1021
    • Galvez, E.1    Duser, M.2    Borsch, M.3    Wrachtrup, J.4    Graber, P.5
  • 47
    • 79954513649 scopus 로고    scopus 로고
    • Subunit rotation in a single F[sub o]F[sub 1]-ATP synthase in a living bacterium monitored by FRET
    • Seyfert, K., Oosaka, T., Yaginuma, H., Ernst, S., Noji, H., Iino, R., and Borsch, M., "Subunit rotation in a single F[sub o]F[sub 1]-ATP synthase in a living bacterium monitored by FRET," Proc. SPIE 7905, 79050K (2011).
    • (2011) Proc. SPIE , vol.7905
    • Seyfert, K.1    Oosaka, T.2    Yaginuma, H.3    Ernst, S.4    Noji, H.5    Iino, R.6    Borsch, M.7
  • 48
    • 84871676748 scopus 로고    scopus 로고
    • Twisting and subunit rotation in single FOF1-ATP synthase
    • Sielaff, H., and Borsch, M., "Twisting and subunit rotation in single FOF1-ATP synthase," Phil Trans R Soc B 368, 20120024 (2012).
    • (2012) Phil Trans R Soc B , vol.368 , pp. 20120024
    • Sielaff, H.1    Borsch, M.2
  • 49
    • 84859085008 scopus 로고    scopus 로고
    • Diffusion properties of single FoF1-ATP synthases in a living bacterium unraveled by localization microscopy
    • Renz, M., Rendler, T., and Borsch, M., "Diffusion properties of single FoF1-ATP synthases in a living bacterium unraveled by localization microscopy," Proc. SPIE 8225, 822513 (2012).
    • (2012) Proc. SPIE , vol.8225 , pp. 822513
    • Renz, M.1    Rendler, T.2    Borsch, M.3
  • 50
    • 84859592536 scopus 로고    scopus 로고
    • Monitoring transient elastic energy storage within the rotary motors of single FoF1-ATP synthase by DCO-ALEX FRET
    • Ernst, S., Duser, M.G., Zarrabi, N., and Borsch, M., "Monitoring transient elastic energy storage within the rotary motors of single FoF1-ATP synthase by DCO-ALEX FRET," Proc. SPIE 8226, 82260I (2012).
    • (2012) Proc. SPIE , vol.8226
    • Ernst, S.1    Duser, M.G.2    Zarrabi, N.3    Borsch, M.4
  • 51
    • 84857551617 scopus 로고    scopus 로고
    • Step size of the rotary proton motor in single FoF1-ATP synthase from a thermoalkaliphilic bacterium by DCO-ALEX FRET
    • Hammann, E., Zappe, A., Keis, S., Ernst, S., Matthies, D., Meier, T., Cook, G.M., and Borsch, M., "Step size of the rotary proton motor in single FoF1-ATP synthase from a thermoalkaliphilic bacterium by DCO-ALEX FRET," Proc. SPIE 8228, 82280A (2012).
    • (2012) Proc. SPIE , vol.8228
    • Hammann, E.1    Zappe, A.2    Keis, S.3    Ernst, S.4    Matthies, D.5    Meier, T.6    Cook, G.M.7    Borsch, M.8
  • 52
    • 21844469231 scopus 로고    scopus 로고
    • The anti-Brownian electrophoretic trap (ABEL trap): Fabrication and software
    • Cohen, A.E., and Moerner, W.E., "The anti-Brownian electrophoretic trap (ABEL trap): fabrication and software," Proc. SPIE 5699, 296-305 (2005).
    • (2005) Proc. SPIE , vol.5699 , pp. 296-305
    • Cohen, A.E.1    Moerner, W.E.2
  • 53
    • 31844442904 scopus 로고    scopus 로고
    • An all-glass microfluidic cell for the ABEL trap: Fabrication and modeling
    • Cohen, A.E., and Moerner, W.E., "An all-glass microfluidic cell for the ABEL trap: fabrication and modeling," Proc. SPIE 5930, 59300S (2005).
    • (2005) Proc. SPIE , vol.5930
    • Cohen, A.E.1    Moerner, W.E.2
  • 54
    • 21044459540 scopus 로고    scopus 로고
    • Method for trapping and manipulating nanoscale objects in solution
    • Cohen, A.E., and Moerner, W.E., "Method for trapping and manipulating nanoscale objects in solution," Appl. Phys. Lett. 86, 093109 (2005).
    • (2005) Appl. Phys. Lett. , vol.86 , pp. 093109
    • Cohen, A.E.1    Moerner, W.E.2
  • 55
    • 43849086810 scopus 로고    scopus 로고
    • Controlling Brownian motion of single protein molecules and single fluorophores in aqueous buffer
    • Cohen, A.E., and Moerner, W.E., "Controlling Brownian motion of single protein molecules and single fluorophores in aqueous buffer," Opt Express 16, 6941-6956 (2008).
    • (2008) Opt Express , vol.16 , pp. 6941-6956
    • Cohen, A.E.1    Moerner, W.E.2
  • 56
    • 79959361906 scopus 로고    scopus 로고
    • Electrokinetic trapping at the one nanometer limit
    • Fields, A.P., and Cohen, A.E., "Electrokinetic trapping at the one nanometer limit," Proc Natl Acad Sci U S A 108, 8937-8942 (2011).
    • (2011) Proc Natl Acad Sci U S A , vol.108 , pp. 8937-8942
    • Fields, A.P.1    Cohen, A.E.2
  • 57
    • 77649101065 scopus 로고    scopus 로고
    • Watching conformational- and photodynamics of single fluorescent proteins in solution
    • Goldsmith, R.H., and Moerner, W.E., "Watching conformational- and photodynamics of single fluorescent proteins in solution," Nat Chem 2, 179-186 (2010).
    • (2010) Nat Chem , vol.2 , pp. 179-186
    • Goldsmith, R.H.1    Moerner, W.E.2
  • 58
    • 80855128957 scopus 로고    scopus 로고
    • Conformational dynamics of single G protein-coupled receptors in solution
    • Bockenhauer, S., Furstenberg, A., Yao, X.J., Kobilka, B.K., and Moerner, W.E., "Conformational dynamics of single G protein-coupled receptors in solution," J Phys Chem B 115, 13328-13338 (2011).
    • (2011) J Phys Chem B , vol.115 , pp. 13328-13338
    • Bockenhauer, S.1    Furstenberg, A.2    Yao, X.J.3    Kobilka, B.K.4    Moerner, W.E.5
  • 59
    • 79961074741 scopus 로고    scopus 로고
    • An Adaptive Anti-Brownian ELectrokinetic trap with real-time information on single-molecule diffusivity and mobility
    • Wang, Q., and Moerner, W.E., "An Adaptive Anti-Brownian ELectrokinetic trap with real-time information on single-molecule diffusivity and mobility," ACS Nano 5, 5792-5799 (2011).
    • (2011) ACS Nano , vol.5 , pp. 5792-5799
    • Wang, Q.1    Moerner, W.E.2
  • 60
    • 0032540490 scopus 로고    scopus 로고
    • Stability and functionality of cysteine-less F(0)F1 ATP synthase from Escherichia coli
    • Kuo, P.H., Ketchum, C.J., and Nakamoto, R.K., "Stability and functionality of cysteine-less F(0)F1 ATP synthase from Escherichia coli," FEBS Lett 426, 217-220 (1998).
    • (1998) FEBS Lett , vol.426 , pp. 217-220
    • Kuo, P.H.1    Ketchum, C.J.2    Nakamoto, R.K.3
  • 61
    • 0026577596 scopus 로고
    • Introduction of reactive cysteine residues in the. epsilon. subunit of Escherichia coli F1 ATPase, modification of these sites with (azidotetrafluorophenyl)maleimides, and examination of changes in the binding of the. epsilon. subunit when different nucleotides are in catalytic sites
    • Aggeler, R., Chicas-Cruz, K., Cai, S.X., Keana, J.F.W., and Capaldi, R.A., "Introduction of reactive cysteine residues in the. epsilon. subunit of Escherichia coli F1 ATPase, modification of these sites with (azidotetrafluorophenyl)maleimides, and examination of changes in the binding of the. epsilon. subunit when different nucleotides are in catalytic sites," Biochemistry 31, 2956-2961 (1992).
    • (1992) Biochemistry , vol.31 , pp. 2956-2961
    • Aggeler, R.1    Chicas-Cruz, K.2    Cai, S.X.3    Keana, J.F.W.4    Capaldi, R.A.5
  • 62
    • 0031202120 scopus 로고    scopus 로고
    • Rotation of a gamma-epsilon subunit domain in the Escherichia coli F1F0-ATP synthase complex. The gamma-epsilon subunits are essentially randomly distributed relative to the alpha3beta3delta domain in the intact complex
    • Aggeler, R., Ogilvie, I., and Capaldi, R.A., "Rotation of a gamma-epsilon subunit domain in the Escherichia coli F1F0-ATP synthase complex. The gamma-epsilon subunits are essentially randomly distributed relative to the alpha3beta3delta domain in the intact complex," J Biol Chem 272, 19621-19624 (1997).
    • (1997) J Biol Chem , vol.272 , pp. 19621-19624
    • Aggeler, R.1    Ogilvie, I.2    Capaldi, R.A.3
  • 63
    • 0025340556 scopus 로고
    • Site-directed mutagenesis of the conserved beta subunit tyrosine 331 of Escherichia coli ATP synthase yields catalytically active enzymes
    • Wise, J.G., "Site-directed mutagenesis of the conserved beta subunit tyrosine 331 of Escherichia coli ATP synthase yields catalytically active enzymes," J Biol Chem 265, 10403-10409 (1990).
    • (1990) J Biol Chem , vol.265 , pp. 10403-10409
    • Wise, J.G.1
  • 64
    • 0018801553 scopus 로고
    • Tightly bound magnesium in mitochondrial adenosine triphosphatase from beef heart
    • Senior, A.E., "Tightly bound magnesium in mitochondrial adenosine triphosphatase from beef heart," Journal of Biological Chemistry 254, 11319-11322 (1979).
    • (1979) Journal of Biological Chemistry , vol.254 , pp. 11319-11322
    • Senior, A.E.1
  • 65
    • 3342922088 scopus 로고
    • A Microcolorimetric Method for the Determination of Inorganic Phosphorus
    • Taussky, H.H., and Shorr, E., "A Microcolorimetric Method for the Determination of Inorganic Phosphorus," Journal of Biological Chemistry 202, 675-685 (1953).
    • (1953) Journal of Biological Chemistry , vol.202 , pp. 675-685
    • Taussky, H.H.1    Shorr, E.2
  • 66
    • 0015384891 scopus 로고
    • Determination of protein: A modification of the lowry method that gives a linear photometric response
    • Hartree, E.F., "Determination of protein: A modification of the lowry method that gives a linear photometric response," Anal Biochem 48, 422-427 (1972).
    • (1972) Anal Biochem , vol.48 , pp. 422-427
    • Hartree, E.F.1
  • 67
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa
    • Schagger, H., and von Jagow, G., "Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa," Anal Biochem 166, 368-379 (1987).
    • (1987) Anal Biochem , vol.166 , pp. 368-379
    • Schagger, H.1    Von Jagow, G.2
  • 68
    • 0021988172 scopus 로고
    • Simplified Method for Silver Staining of Proteins in Polyacrylamide Gels and the Mechanism of Silver Staining
    • Heukeshoven, J., and Dernick, R., "Simplified Method for Silver Staining of Proteins in Polyacrylamide Gels and the Mechanism of Silver Staining," Electrophoresis 6, 103-112 (1985).
    • (1985) Electrophoresis , vol.6 , pp. 103-112
    • Heukeshoven, J.1    Dernick, R.2
  • 69
    • 0038245730 scopus 로고    scopus 로고
    • Catalytic site nucleotide binding and hydrolysis in F1F0-ATP synthase
    • Lobau, S., Weber, J., and Senior, A.E., "Catalytic site nucleotide binding and hydrolysis in F1F0-ATP synthase," Biochemistry 37, 10846-10853 (1998).
    • (1998) Biochemistry , vol.37 , pp. 10846-10853
    • Lobau, S.1    Weber, J.2    Senior, A.E.3
  • 70
    • 33746747438 scopus 로고    scopus 로고
    • Analysis of single-molecule FRET trajectories using hidden Markov modeling
    • McKinney, S.A., Joo, C., and Ha, T., "Analysis of single-molecule FRET trajectories using hidden Markov modeling," Biophys J 91, 1941-1951 (2006).
    • (2006) Biophys J , vol.91 , pp. 1941-1951
    • McKinney, S.A.1    Joo, C.2    Ha, T.3
  • 71
    • 40849083594 scopus 로고    scopus 로고
    • K(+)-Translocating KdpFABC PType ATPase from Escherichia coli Acts as a Functional and Structural Dimer
    • Heitkamp, T., Kalinowski, R., Bottcher, B., Borsch, M., Altendorf, K., and Greie, J.C., "K(+)-Translocating KdpFABC PType ATPase from Escherichia coli Acts as a Functional and Structural Dimer," Biochemistry 47, 3564-3575 (2008).
    • (2008) Biochemistry , vol.47 , pp. 3564-3575
    • Heitkamp, T.1    Kalinowski, R.2    Bottcher, B.3    Borsch, M.4    Altendorf, K.5    Greie, J.C.6
  • 72
    • 15544385722 scopus 로고    scopus 로고
    • Evidence for major structural changes in subunit C of the vacuolar ATPase due to nucleotide binding
    • Armbruster, A., Hohn, C., Hermesdorf, A., Schumacher, K., Borsch, M., and Gruber, G., "Evidence for major structural changes in subunit C of the vacuolar ATPase due to nucleotide binding," FEBS Lett 579, 1961-1967 (2005).
    • (2005) FEBS Lett , vol.579 , pp. 1961-1967
    • Armbruster, A.1    Hohn, C.2    Hermesdorf, A.3    Schumacher, K.4    Borsch, M.5    Gruber, G.6
  • 73
    • 84855476209 scopus 로고    scopus 로고
    • Dynamic ligand induced conformational rearrangements in Pglycoprotein as probed by fluorescence resonance energy transfer spectroscopy
    • Verhalen, B., Ernst, S., Borsch, M., and Wilkens, S., "Dynamic ligand induced conformational rearrangements in Pglycoprotein as probed by fluorescence resonance energy transfer spectroscopy," Journal of Biological Chemistry 287, 1112-1127 (2012).
    • (2012) Journal of Biological Chemistry , vol.287 , pp. 1112-1127
    • Verhalen, B.1    Ernst, S.2    Borsch, M.3    Wilkens, S.4
  • 74
    • 53849140811 scopus 로고    scopus 로고
    • Structural organization of the V-ATPase and its implications for regulatory assembly and disassembly
    • Diepholz, M., Borsch, M., and Bottcher, B., "Structural organization of the V-ATPase and its implications for regulatory assembly and disassembly," Biochem Soc Trans 36, 1027-1031 (2008).
    • (2008) Biochem Soc Trans , vol.36 , pp. 1027-1031
    • Diepholz, M.1    Borsch, M.2    Bottcher, B.3
  • 76
    • 67650499134 scopus 로고    scopus 로고
    • Diffusion in Model Networks as Studied by NMR and Fluorescence Correlation Spectroscopy
    • Modesti, G., Zimmermann, B., Borsch, M., Herrmann, A., and Saalwachter, K., "Diffusion in Model Networks as Studied by NMR and Fluorescence Correlation Spectroscopy," Macromolecules 42, 4681-4689 (2009).
    • (2009) Macromolecules , vol.42 , pp. 4681-4689
    • Modesti, G.1    Zimmermann, B.2    Borsch, M.3    Herrmann, A.4    Saalwachter, K.5
  • 77
    • 77951734915 scopus 로고    scopus 로고
    • Regulatory assembly of the vacuolar proton pump VoV1- ATPase in yeast cells by FLIM-FRET
    • Ernst, S., Batisse, C., Zarrabi, N., Bottcher, B., and Borsch, M., "Regulatory assembly of the vacuolar proton pump VoV1- ATPase in yeast cells by FLIM-FRET," Proc. SPIE 7569, 75690W (2010).
    • (2010) Proc. SPIE , vol.7569
    • Ernst, S.1    Batisse, C.2    Zarrabi, N.3    Bottcher, B.4    Borsch, M.5
  • 78
    • 80052033226 scopus 로고    scopus 로고
    • YidC-driven membrane insertion of single fluorescent Pf3 coat proteins
    • Ernst, S., Schonbauer, A.K., Bar, G., Borsch, M., and Kuhn, A., "YidC-driven membrane insertion of single fluorescent Pf3 coat proteins," J Mol Biol 412, 165-175 (2011).
    • (2011) J Mol Biol , vol.412 , pp. 165-175
    • Ernst, S.1    Schonbauer, A.K.2    Bar, G.3    Borsch, M.4    Kuhn, A.5
  • 79
    • 79955493449 scopus 로고    scopus 로고
    • Drug transport mechanism of P-glycoprotein monitored by single molecule fluorescence resonance energy transfer
    • Ernst, S., Verhalen, B., Zarrabi, N., Wilkens, S., and Borsch, M., "Drug transport mechanism of P-glycoprotein monitored by single molecule fluorescence resonance energy transfer," Proc. SPIE 7903, 790328 (2011).
    • (2011) Proc. SPIE , vol.7903 , pp. 790328
    • Ernst, S.1    Verhalen, B.2    Zarrabi, N.3    Wilkens, S.4    Borsch, M.5
  • 80
    • 77954591428 scopus 로고    scopus 로고
    • Anti-Brownian traps for studies on single molecules
    • Fields, A.P., and Cohen, A.E., "Anti-Brownian traps for studies on single molecules," Methods Enzymol 475, 149-174 (2010).
    • (2010) Methods Enzymol , vol.475 , pp. 149-174
    • Fields, A.P.1    Cohen, A.E.2
  • 81
    • 79954496524 scopus 로고    scopus 로고
    • Monitoring single membrane protein dynamics in a liposome manipulated in solution by the ABELtrap
    • Rendler, T., Renz, M., Hammann, E., Ernst, S., Zarrabi, N., and Borsch, M., "Monitoring single membrane protein dynamics in a liposome manipulated in solution by the ABELtrap," Proc. SPIE 7902, 79020M (2011).
    • (2011) Proc. SPIE , vol.7902
    • Rendler, T.1    Renz, M.2    Hammann, E.3    Ernst, S.4    Zarrabi, N.5    Borsch, M.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.