메뉴 건너뛰기




Volumn 98, Issue 4, 2010, Pages 696-706

Distinguishing between protein dynamics and dye photophysics in single-molecule FRET experiments

Author keywords

[No Author keywords available]

Indexed keywords

ALEXA;

EID: 77249133072     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1016/j.bpj.2009.12.4322     Document Type: Article
Times cited : (52)

References (30)
  • 1
    • 0029987587 scopus 로고    scopus 로고
    • Probing the interaction between two single molecules: Fluorescence resonance energy transfer between a single donor and a single acceptor
    • Ha, T., T. Enderle, ..., S. Weiss. 1996. Probing the interaction between two single molecules: fluorescence resonance energy transfer between a single donor and a single acceptor. Proc. Natl. Acad. Sci. USA. 93:6264-6268.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 6264-6268
    • Ha, T.1    Enderle, T.2    Weiss, S.3
  • 2
    • 0034807927 scopus 로고    scopus 로고
    • Single-molecule fluorescence resonance energy transfer
    • Ha, T. 2001. Single-molecule fluorescence resonance energy transfer. Methods. 25:78-86.
    • (2001) Methods , vol.25 , pp. 78-86
    • Ha, T.1
  • 3
    • 39149087014 scopus 로고    scopus 로고
    • Protein folding studied by singlemolecule FRET
    • Schuler, B., and W. A. Eaton. 2008. Protein folding studied by singlemolecule FRET. Curr. Opin. Struct. Biol. 18:16-26.
    • (2008) Curr. Opin. Struct. Biol , vol.18 , pp. 16-26
    • Schuler, B.1    Eaton, W.A.2
  • 4
    • 37649015345 scopus 로고    scopus 로고
    • Effect of flexibility and cis residues in single-molecule FRET studies of polyproline
    • Best, R. B., K. A. Merchant, ..., W. A. Eaton. 2007. Effect of flexibility and cis residues in single-molecule FRET studies of polyproline. Proc. Natl. Acad. Sci. USA. 104:18964-18969.
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 18964-18969
    • Best, R.B.1    Merchant, K.A.2    Eaton, W.A.3
  • 5
    • 33846839535 scopus 로고    scopus 로고
    • Characterizing the unfolded states of proteins using single-molecule FRET spectroscopy and molecular simulations
    • Merchant, K. A., R. B. Best, ..., W. A. Eaton. 2007. Characterizing the unfolded states of proteins using single-molecule FRET spectroscopy and molecular simulations. Proc. Natl. Acad. Sci. USA. 104: 1528-1533.
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 1528-1533
    • Merchant, K.A.1    Best, R.B.2    Eaton, W.A.3
  • 6
    • 34548096938 scopus 로고    scopus 로고
    • Theory of photon statistics in singlemolecule Fö rster resonance energy transfer
    • Gopich, I., and A. Szabo. 2005. Theory of photon statistics in singlemolecule Fö rster resonance energy transfer. J. Chem. Phys. 122:014707.
    • (2005) J. Chem. Phys , vol.122 , pp. 014707
    • Gopich, I.1    Szabo, A.2
  • 7
    • 36249028655 scopus 로고    scopus 로고
    • Single-molecule FRET with diffusion and conformational dynamics
    • Gopich, I. V., and A. Szabo. 2007. Single-molecule FRET with diffusion and conformational dynamics. J. Phys. Chem. B. 111:12925-12932.
    • (2007) J. Phys. Chem. B , vol.111 , pp. 12925-12932
    • Gopich, I.V.1    Szabo, A.2
  • 8
    • 79955425093 scopus 로고    scopus 로고
    • Theory of single-molecule fluorescence resonance energy transfer histograms
    • In press
    • Gopich, I., and A. Szabo. 2009. Theory of single-molecule fluorescence resonance energy transfer histograms. Adv. Chem. Phys. In press.
    • (2009) Adv. Chem. Phys
    • Gopich, I.1    Szabo, A.2
  • 9
    • 33751349660 scopus 로고    scopus 로고
    • Shot-noise limited singlemolecule FRET histograms: Comparison between theory and experiments
    • Nir, E., X. Michalet, ..., S. Weiss. 2006. Shot-noise limited singlemolecule FRET histograms: comparison between theory and experiments. J. Phys. Chem. B. 110:22103-22124.
    • (2006) J. Phys. Chem. B , vol.110 , pp. 22103-22124
    • Nir, E.1    Michalet, X.2    Weiss, S.3
  • 10
    • 0034625167 scopus 로고    scopus 로고
    • Single-molecule protein folding: Diffusion fluorescence resonance energy transfer studies of the denaturation of chymotrypsin inhibitor 2
    • Deniz, A. A., T. A. Laurence, ..., S. Weiss. 2000. Single-molecule protein folding: diffusion fluorescence resonance energy transfer studies of the denaturation of chymotrypsin inhibitor 2. Proc. Natl. Acad. Sci. USA. 97:5179-5184.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 5179-5184
    • Deniz, A.A.1    Laurence, T.A.2    Weiss, S.3
  • 11
    • 1542501215 scopus 로고    scopus 로고
    • Dynamics and folding of single two-stranded coiled-coil peptides studied by fluorescent energy transfer confocal microscopy
    • Talaga, D. S., W. L. Lau, ..., R. M. Hochstrasser. 2000. Dynamics and folding of single two-stranded coiled-coil peptides studied by fluorescent energy transfer confocal microscopy. Proc. Natl. Acad. Sci. USA. 97:13021-13026.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 13021-13026
    • Talaga, D.S.1    Lau, W.L.2    Hochstrasser, R.M.3
  • 12
    • 0037126290 scopus 로고    scopus 로고
    • Probing the freeenergy surface for protein folding with single-molecule fluorescence spectroscopy
    • Schuler, B., E. A. Lipman, and W. A. Eaton. 2002. Probing the freeenergy surface for protein folding with single-molecule fluorescence spectroscopy. Nature. 419:743-747.
    • (2002) Nature , vol.419 , pp. 743-747
    • Schuler, B.1    Lipman, E.A.2    Eaton, W.A.3
  • 13
    • 27344452885 scopus 로고    scopus 로고
    • Singlemolecule Forster resonance energy transfer study of protein dynamics under denaturing conditions
    • Kuzmenkina, E. V., C. D. Heyes, and G. U. Nienhaus. 2005. Singlemolecule Forster resonance energy transfer study of protein dynamics under denaturing conditions. Proc. Natl. Acad. Sci. USA. 102:15471-15476.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 15471-15476
    • Kuzmenkina, E.V.1    Heyes, C.D.2    Nienhaus, G.U.3
  • 14
    • 67650069580 scopus 로고    scopus 로고
    • Fluorescence quenching by photoinduced electron transfer: A reporter for conformational dynamics of macromolecules
    • Doose, S., H. Neuweiler, and M. Sauer. 2009. Fluorescence quenching by photoinduced electron transfer: a reporter for conformational dynamics of macromolecules. ChemPhysChem. 10:1389-1398.
    • (2009) ChemPhysChem , vol.10 , pp. 1389-1398
    • Doose, S.1    Neuweiler, H.2    Sauer, M.3
  • 15
    • 34547529763 scopus 로고    scopus 로고
    • Dynamics of equilibrium structural fluctuations of apomyoglobin measured by fluorescence correlation spectroscopy
    • Chen, H. M., E. Rhoades, ..., W. W. Webb. 2007. Dynamics of equilibrium structural fluctuations of apomyoglobin measured by fluorescence correlation spectroscopy. Proc. Natl. Acad. Sci. USA. 104:10459-10464.
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 10459-10464
    • Chen, H.M.1    Rhoades, E.2    Webb, W.W.3
  • 16
    • 6444240770 scopus 로고    scopus 로고
    • II-quenched oligonucleotide probes for fluorescent DNA sensing
    • II-quenched oligonucleotide probes for fluorescent DNA sensing. J. Am. Chem. Soc. 126:13626-13627.
    • (2004) J. Am. Chem. Soc , vol.126 , pp. 13626-13627
    • Brunner, J.1    Kraemer, R.2
  • 18
    • 70349762917 scopus 로고    scopus 로고
    • Nanoparticle PEBBLE sensors in live cells and in vivo
    • Lee, Y. E. K., R. Smith, and R. Kopelman. 2009. Nanoparticle PEBBLE sensors in live cells and in vivo. Ann. Rev. Anal. Chem. 2:57-76.
    • (2009) Ann. Rev. Anal. Chem , vol.2 , pp. 57-76
    • Lee, Y.E.K.1    Smith, R.2    Kopelman, R.3
  • 19
    • 67749147584 scopus 로고    scopus 로고
    • Experimental determination of upper bound for transition path times in protein folding from single-molecule photon-by-photon trajectories
    • Chung, H. S., J. M. Louis, and W. A. Eaton. 2009. Experimental determination of upper bound for transition path times in protein folding from single-molecule photon-by-photon trajectories. Proc. Natl. Acad. Sci. USA. 106:11837-11844.
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 11837-11844
    • Chung, H.S.1    Louis, J.M.2    Eaton, W.A.3
  • 20
    • 18844471887 scopus 로고    scopus 로고
    • Identification of single molecules in aqueous solution by time-resolved fluorescence anisotropy
    • Schaffer, J., A. Volkmer, ..., C. A. M. Seidel. 1999. Identification of single molecules in aqueous solution by time-resolved fluorescence anisotropy. J. Phys. Chem. A. 103:331-336.
    • (1999) J. Phys. Chem. A , vol.103 , pp. 331-336
    • Schaffer, J.1    Volkmer, A.2    Seidel, C.A.M.3
  • 21
    • 44949240469 scopus 로고    scopus 로고
    • Unfolded protein and peptide dynamics investigated with single-molecule FRET and correlation spectroscopy from picoseconds to seconds
    • Nettels, D., A. Hoffmann, and B. Schuler. 2008. Unfolded protein and peptide dynamics investigated with single-molecule FRET and correlation spectroscopy from picoseconds to seconds. J. Phys. Chem. B. 112:6137-6146.
    • (2008) J. Phys. Chem. B , vol.112 , pp. 6137-6146
    • Nettels, D.1    Hoffmann, A.2    Schuler, B.3
  • 23
    • 33646796290 scopus 로고    scopus 로고
    • Effects of denaturants on the dynamics of loop formation in polypeptides
    • Buscaglia, M., L. J. Lapidus, ..., J. Hofrichter. 2006. Effects of denaturants on the dynamics of loop formation in polypeptides. Biophys. J. 91:276-288.
    • (2006) Biophys. J , vol.91 , pp. 276-288
    • Buscaglia, M.1    Lapidus, L.J.2    Hofrichter, J.3
  • 24
    • 0026513046 scopus 로고
    • Nature of biological electron transfer
    • Moser, C. C., J. M. Keske, ..., P. L. Dutton. 1992. Nature of biological electron transfer. Nature. 355:796-802.
    • (1992) Nature , vol.355 , pp. 796-802
    • Moser, C.C.1    Keske, J.M.2    Dutton, P.L.3
  • 25
    • 0037038514 scopus 로고    scopus 로고
    • Effects of chain stiffness on the dynamics of loop formation in polypeptides
    • Lapidus, L. J., P. J. Steinbach, ..., J. Hofrichter. 2002. Effects of chain stiffness on the dynamics of loop formation in polypeptides. J. Phys. Chem. B. 106:11628-11640.
    • (2002) J. Phys. Chem. B , vol.106 , pp. 11628-11640
    • Lapidus, L.J.1    Steinbach, P.J.2    Hofrichter, J.3
  • 26
    • 33747623305 scopus 로고    scopus 로고
    • End-to-end distance distributions and intrachain diffusion constants in unfolded polypeptide chains indicate intramolecular hydrogen bond formation
    • Mö glich, A., K. Joder, and T. Kiefhaber. 2006. End-to-end distance distributions and intrachain diffusion constants in unfolded polypeptide chains indicate intramolecular hydrogen bond formation. Proc. Natl. Acad. Sci. USA. 103:12394-12399.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 12394-12399
    • Mö glich, A.1    Joder, K.2    Kiefhaber, T.3
  • 27
    • 33847254454 scopus 로고    scopus 로고
    • Ultrafast dynamics of protein collapse from single-molecule photon statistics
    • Nettels, D., I. V. Gopich, ..., B. Schuler. 2007. Ultrafast dynamics of protein collapse from single-molecule photon statistics. Proc. Natl. Acad. Sci. USA. 104:2655-2660.
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 2655-2660
    • Nettels, D.1    Gopich, I.V.2    Schuler, B.3
  • 28
    • 14344280947 scopus 로고
    • Changes in fluorescence lifetimes induced by variable optical environments
    • Kunz, R. E., and W. Lukosz. 1980. Changes in fluorescence lifetimes induced by variable optical environments. Phys. Rev. B. 21:4814-4828.
    • (1980) Phys. Rev. B , vol.21 , pp. 4814-4828
    • Kunz, R.E.1    Lukosz, W.2
  • 29
    • 0000793711 scopus 로고    scopus 로고
    • Imaging and timeresolved spectroscopy of single molecules at an interface
    • Macklin, J. J., J. K. Trautman, ..., L. E. Brus. 1996. Imaging and timeresolved spectroscopy of single molecules at an interface. Science. 272:255-258.
    • (1996) Science , vol.272 , pp. 255-258
    • Macklin, J.J.1    Trautman, J.K.2    Brus, L.E.3
  • 30
    • 0037182960 scopus 로고    scopus 로고
    • Fluorescence quenching and lifetime distributions of single molecules on glass surfaces
    • Lee, M., J. Kim, ..., R. M. Hochstrasser. 2002. Fluorescence quenching and lifetime distributions of single molecules on glass surfaces. Chem. Phys. Lett. 359:412-419.
    • (2002) Chem. Phys. Lett , vol.359 , pp. 412-419
    • Lee, M.1    Kim, J.2    Hochstrasser, R.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.