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Volumn 3, Issue 1, 2010, Pages 319-340

Single-biomolecule kinetics: The art of studying a single enzyme

Author keywords

bioencapsulation; enzyme kinetics; protein immobilization; single molecule microscopy

Indexed keywords

ANALYSIS METHOD; BIOENCAPSULATION; BIOLOGICAL FUNCTIONS; CATALYTIC RATES; COMPLEX ENERGY LANDSCAPES; CONFORMATIONAL FLUCTUATIONS; CRITICAL STEPS; ENERGY LANDSCAPE; ENZYMATIC TURNOVER; ENZYME MOLECULES; EXPERIMENTAL TECHNIQUES; POLYMERIC CATALYSTS; PROTEIN IMMOBILIZATION; SINGLE-MOLECULE; SINGLE-MOLECULE MICROSCOPY; STATIC AND DYNAMIC DISORDER; TECHNOLOGICAL ADVANCES; TIME RESOLUTION; TIME-RESOLVED;

EID: 78049383225     PISSN: 19361327     EISSN: 19361335     Source Type: Book Series    
DOI: 10.1146/annurev.anchem.111808.073638     Document Type: Article
Times cited : (47)

References (80)
  • 1
    • 0000870544 scopus 로고
    • Die kinetik der invertinwirkung
    • Michaelis L, Menten ML. 1913. Die Kinetik der Invertinwirkung. Biochem. Z. 49:333-69
    • (1913) Biochem. Z. , vol.49 , pp. 333-369
    • Michaelis, L.1    Menten, M.L.2
  • 2
    • 78651119908 scopus 로고
    • Measurement of activity of single molecules of ß-D-galactosidase
    • USA
    • Rotman B. 1961. Measurement of activity of single molecules of ß-D-galactosidase. Proc. Natl. Acad. Sci. USA 47:1981-91
    • (1961) Proc. Natl. Acad. Sci. , vol.47 , pp. 1981-1991
    • Rotman, B.1
  • 3
    • 0028907107 scopus 로고
    • Proteins-paradigms of complex systems
    • Frauenfelder H. 1995. Proteins-paradigms of complex systems. Experientia 51:200-3
    • (1995) Experientia , vol.51 , pp. 200-203
    • Frauenfelder, H.1
  • 4
    • 37249032102 scopus 로고    scopus 로고
    • Dynamic personalities of proteins
    • DOI 10.1038/nature06522, PII NATURE06522
    • Henzler-Wildman K, Kern D. 2007. Dynamic personalities of proteins. Nature 450:964-72 (Pubitemid 350273626)
    • (2007) Nature , vol.450 , Issue.7172 , pp. 964-972
    • Henzler-Wildman, K.1    Kern, D.2
  • 5
    • 14644435825 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins and their functions
    • DOI 10.1038/nrm1589
    • Dyson HJ, Wright PE. 2005. Intrinsically unstructured proteins and their functions. Nat. Rev. Mol. Cell Biol. 6:197-208 (Pubitemid 40314921)
    • (2005) Nature Reviews Molecular Cell Biology , vol.6 , Issue.3 , pp. 197-208
    • Dyson, H.J.1    Wright, P.E.2
  • 6
    • 34250821717 scopus 로고    scopus 로고
    • Mechanism of coupled folding and binding of an intrinsically disordered protein
    • DOI 10.1038/nature05858, PII NATURE05858
    • Sugase K, Dyson HJ, Wright PE. 2007. Mechanism of coupled folding and binding of an intrinsically disordered protein. Nature 447:1021-25 (Pubitemid 46975749)
    • (2007) Nature , vol.447 , Issue.7147 , pp. 1021-1025
    • Sugase, K.1    Dyson, H.J.2    Wright, P.E.3
  • 7
    • 33748799981 scopus 로고    scopus 로고
    • Dynamic visions of enzymatic reactions
    • DOI 10.1126/science.1132851
    • Vendruscolo M, Dobson CM. 2006. Dynamic visions of enzymatic reactions. Science 313:1586-87 (Pubitemid 44414023)
    • (2006) Science , vol.313 , Issue.5793 , pp. 1586-1587
    • Vendruscolo, M.1    Dobson, C.M.2
  • 8
    • 0032484096 scopus 로고    scopus 로고
    • Single-molecule enzymatic dynamics
    • Lu HP, Xun L, Xie XS. 1998. Single-molecule enzymatic dynamics. Science 282:1877-82
    • (1998) Science , vol.282 , pp. 1877-1882
    • Lu, H.P.1    Xun, L.2    Xie, X.S.3
  • 13
    • 33644910749 scopus 로고    scopus 로고
    • Ever-fluctuating single enzymemolecules: Michaelis-menten equation revisited
    • English BP, MinW, van OijenAM, LeeKT, Luo G, et al. 2006. Ever-fluctuating single enzymemolecules: Michaelis-Menten equation revisited. Nat. Chem. Biol. 2:87-94
    • (2006) Nat. Chem. Biol. , vol.2 , pp. 87-94
    • English, B.P.1    Min, W.2    Van Oijen, A.M.3    Lee, K.T.4    Luo, G.5
  • 15
    • 42149136142 scopus 로고    scopus 로고
    • Distinct and long-lived activity states of single enzymemolecules
    • RissinDM, Gorris HH, Walt DR. 2008. Distinct and long-lived activity states of single enzymemolecules. J. Am. Chem. Soc. 130:5349-53
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 5349-5353
    • Rissin, D.M.1    Gorris, H.H.2    Walt, D.R.3
  • 16
    • 0037154884 scopus 로고    scopus 로고
    • Enzyme dynamics during catalysis
    • DOI 10.1126/science.1066176
    • Eisenmesser EZ, Bosco DA, Akke M, Kern D. 2002. Enzyme dynamics during catalysis. Science 295:1520-23 (Pubitemid 34174006)
    • (2002) Science , vol.295 , Issue.5559 , pp. 1520-1523
    • Eisenmesser, E.Z.1    Bosco, D.A.2    Akke, M.3    Kern, D.4
  • 21
    • 37649010540 scopus 로고    scopus 로고
    • Construction of effective free energy landscape from single-molecule time series
    • USA
    • Baba A, Komatsuzaki T. 2007. Construction of effective free energy landscape from single-molecule time series. Proc. Natl. Acad. Sci. USA 104:19297-302
    • (2007) Proc. Natl. Acad. Sci. , vol.104 , pp. 19297-19302
    • Baba, A.1    Komatsuzaki, T.2
  • 23
    • 6344219895 scopus 로고    scopus 로고
    • Is allostery an intrinsic property of all dynamic proteins
    • GunasekaranK,Ma B,Nussinov R. 2004. Is allostery an intrinsic property of all dynamic proteins? Proteins 57:433-43
    • (2004) Proteins , vol.57 , pp. 433-443
    • Gunasekaran, K.Ma.1    Nussinov, R.2
  • 24
  • 25
    • 45849095234 scopus 로고    scopus 로고
    • How do proteins interact
    • Boehr DD, Wright PE. 2008. How do proteins interact? Science 320:1429-30
    • (2008) Science , vol.320 , pp. 1429-1430
    • Boehr, D.D.1    Wright, P.E.2
  • 26
    • 0035937443 scopus 로고    scopus 로고
    • Two-state allosteric behavior in a single-domain signaling protein
    • DOI 10.1126/science.291.5512.2429
    • Volkman BF, Lipson D, Wemmer DE, Kern D. 2001. Two-state allosteric behavior in a single-domain signaling protein. Science 291:2429-33 (Pubitemid 32231808)
    • (2001) Science , vol.291 , Issue.5512 , pp. 2429-2433
    • Volkman, B.F.1    Lipson, D.2    Wemmer, D.E.3    Kern, D.4
  • 27
    • 33646776723 scopus 로고    scopus 로고
    • Reconciling the old and new views of protein allostery: A molecular simulation study of chemotaxis Y protein CheY
    • Formaneck MS, Ma L, Cui Q. 2006. Reconciling the old and new views of protein allostery: a molecular simulation study of chemotaxis Y protein (CheY). Proteins 63:846-67
    • (2006) Proteins , vol.63 , pp. 846-867
    • Formaneck, M.S.1    Ma, L.2    Cui, Q.3
  • 28
    • 0015505502 scopus 로고
    • Conformational equilibria in α- and d-chymotrypsin the energetics and importance of the salt bridge
    • Fersht AR. 1972. Conformational equilibria in α- and d-chymotrypsin. The energetics and importance of the salt bridge. J. Mol. Biol. 64:497-509
    • (1972) J. Mol. Biol. , vol.64 , pp. 497-509
    • Fersht, A.R.1
  • 29
    • 41049090929 scopus 로고    scopus 로고
    • Macromolecular crowding and confinement: Biochemical biophysical and potential physiological consequences
    • Zhou HX, Rivas G, Minton AP. 2008. Macromolecular crowding and confinement: biochemical, biophysical, and potential physiological consequences. Annu. Rev. Biophys. 37:375-97
    • (2008) Annu. Rev. Biophys. , vol.37 , pp. 375-397
    • Zhou, H.X.1    Rivas, G.2    Minton, A.P.3
  • 30
    • 0038148710 scopus 로고    scopus 로고
    • Conformational diversity and protein evolution - A 60-year-old hypothesis revisited
    • James LC, Tawfik DS. 2003. Conformational diversity and protein evolution-a 60-year-old hypothesis revisited. Trends Biochem. Sci. 28:361-68
    • (2003) Trends Biochem. Sci. , vol.28 , pp. 361-368
    • James, L.C.1    Tawfik, D.S.2
  • 31
    • 0032559298 scopus 로고    scopus 로고
    • Simultaneous observation of individual ATPase and mechanical events by a single myosin molecule during interaction with actin
    • DOI 10.1016/S0092-8674(00)80911-3
    • Ishijima A, Kojima H, Funatsu T, Tokunaga M, Higuchi H, et al. 1998. Simultaneous observation of individual ATPase and mechanical events by a single myosin molecule during interaction with actin. Cell 92:161-71 (Pubitemid 28073040)
    • (1998) Cell , vol.92 , Issue.2 , pp. 161-171
    • Ishijima, A.1    Kojima, H.2    Funatsu, T.3    Tokunaga, M.4    Higuchi, H.5    Tanaka, H.6    Yanagida, T.7
  • 34
    • 33748614065 scopus 로고    scopus 로고
    • Single molecule studies of enzyme mechanisms
    • Smiley RD, Hammes GG. 2006. Single molecule studies of enzyme mechanisms. Chem. Rev. 106:3080-94
    • (2006) Chem. Rev. , vol.106 , pp. 3080-3094
    • Smiley, R.D.1    Hammes, G.G.2
  • 35
    • 65549151735 scopus 로고    scopus 로고
    • Fluorescence-based analysis of enzymes at the single-molecule level
    • Blank K, De Cremer G, Hofkens J. 2009. Fluorescence-based analysis of enzymes at the single-molecule level. Biotechnol. J. 4:465-79
    • (2009) Biotechnol. J. , vol.4 , pp. 465-479
    • Blank, K.1    De Cremer, G.2    Hofkens, J.3
  • 36
    • 31544470401 scopus 로고    scopus 로고
    • Laser absorption scanning tunneling microscopy of carbon nanotubes
    • DOI 10.1021/nl0519231
    • Ballard JB, Carmichael ES, Shi D, Lyding JW, Gruebele M. 2006. Laser absorption scanning tunneling microscopy of carbon nanotubes. Nano Lett. 6:45-49 (Pubitemid 43166101)
    • (2006) Nano Letters , vol.6 , Issue.1 , pp. 45-49
    • Ballard, J.B.1    Carmichael, E.S.2    Shi, D.3    Lyding, J.W.4    Gruebele, M.5
  • 37
    • 0028945654 scopus 로고
    • Imaging of single fluorescent molecules and individual ATP turnovers by single myosin molecules in aqueous solution
    • Funatsu T, Harada Y, Tokunaga M, Saito K, Yanagida T. 1995. Imaging of single fluorescent molecules and individual ATP turnovers by single myosin molecules in aqueous solution. Nature 374:555-59
    • (1995) Nature , vol.374 , pp. 555-559
    • Funatsu, T.1    Harada, Y.2    Tokunaga, M.3    Saito, K.4    Yanagida, T.5
  • 39
    • 34447628890 scopus 로고    scopus 로고
    • 1-ATPase Revealed by Single-Molecule Imaging and Manipulation
    • DOI 10.1016/j.cell.2007.05.020, PII S0092867407006575
    • Adachi K, Oiwa K, Nishizaka T, Furuike S, Noji H, et al. 2007. Coupling of rotation and catalysis in F1-ATPase revealed by single-molecule imaging and manipulation. Cell 130:309-21 (Pubitemid 47086326)
    • (2007) Cell , vol.130 , Issue.2 , pp. 309-321
    • Adachi, K.1    Oiwa, K.2    Nishizaka, T.3    Furuike, S.4    Noji, H.5    Itoh, H.6    Yoshida, M.7    Kinosita Jr., K.8
  • 40
    • 84983965438 scopus 로고
    • Memoir on inventing the confocal scanning microscope
    • Minsky M. 1988. Memoir on inventing the confocal scanning microscope. Scanning 10:128-38
    • (1988) Scanning , vol.10 , pp. 128-138
    • Minsky, M.1
  • 41
    • 35949038838 scopus 로고
    • Thermodynamic fluctuations in a reacting system-measurement by fluorescence correlation spectroscopy
    • Magde D, Elson EL, WebbWW.1972. Thermodynamic fluctuations in a reacting system-measurement by fluorescence correlation spectroscopy. Phys. Rev. Lett. 29:705-8
    • (1972) Phys. Rev. Lett. , vol.29 , pp. 705-708
    • Magde, D.1    Elson, E.L.2    Webb, W.W.3
  • 42
    • 0016366591 scopus 로고
    • Fluorescence correlation spectroscopy II An experimental realization
    • Magde D, Elson EL, Webb WW. 1974. Fluorescence correlation spectroscopy. II. An experimental realization. Biopolymers 13:29-61
    • (1974) Biopolymers , vol.13 , pp. 29-61
    • Magde, D.1    Elson, E.L.2    Webb, W.W.3
  • 43
    • 1542304184 scopus 로고
    • Rotational brownian motion and fluorescence intensity fluctuations
    • Ehrenberg M, Rigler R. 1974. Rotational brownian motion and fluorescence intensity fluctuations. Chem. Phys. 4:390-401
    • (1974) Chem. Phys. , vol.4 , pp. 390-401
    • Ehrenberg, M.1    Rigler, R.2
  • 44
    • 0036175642 scopus 로고    scopus 로고
    • Fluorescence correlation spectroscopy: The technique and its applications
    • Krichevsky O, BonnetG. 2002. Fluorescence correlation spectroscopy: The technique and its applications. Rep. Prog. Phys. 65:251-97
    • (2002) Rep. Prog. Phys. , vol.65 , pp. 251-297
    • Krichevsky, O.1    Bonnet, G.2
  • 45
    • 0023999464 scopus 로고
    • Photon correlation measurements at large lag times: Improving statistical accuracy
    • Schatzel K, Drewel M, Stimac S. 1988. Photon correlation measurements at large lag times: improving statistical accuracy. J. Mod. Opt. 35:711-18 (Pubitemid 18609100)
    • (1988) Journal of Modern Optics , vol.35 , Issue.4 , pp. 711-718
    • Schaetzel Klaus1    Drewel Martin2    Stimac Sven3
  • 46
    • 2942731432 scopus 로고    scopus 로고
    • Fast calculation of fluorescence correlation data with asynchronous time-correlated single-photon counting
    • Wahl M, Gregor I, Patting M, Enderlein J. 2003. Fast calculation of fluorescence correlation data with asynchronous time-correlated single-photon counting. Opt. Express 11:3583-91
    • (2003) Opt. Express , vol.11 , pp. 3583-3591
    • Wahl, M.1    Gregor, I.2    Patting, M.3    Enderlein, J.4
  • 47
    • 33645731917 scopus 로고    scopus 로고
    • Fast flexible algorithm for calculating photon correlations
    • Laurence TA, Fore S, Huser T. 2006. Fast, flexible algorithm for calculating photon correlations. Opt. Lett. 31:829-31
    • (2006) Opt. Lett. , vol.31 , pp. 829-831
    • Laurence, T.A.1    Fore, S.2    Huser, T.3
  • 49
    • 58149520825 scopus 로고    scopus 로고
    • Linking phospholipase mobility to activity by single-molecule wide-field microscopy
    • Rocha S, Hutchison JA, Peneva K, Herrmann A, Müllen K, et al. 2009. Linking phospholipase mobility to activity by single-molecule wide-field microscopy. ChemPhysChem 10:151-61
    • (2009) Chem. Phys. Chem. , vol.10 , pp. 151-161
    • Rocha, S.1    Hutchison, J.A.2    Peneva, K.3    Herrmann, A.4    Müllen, K.5
  • 50
    • 58249114971 scopus 로고    scopus 로고
    • Dynamics of DNA replication loops reveal temporal control of lagging-strand synthesis
    • Hamdan SM, Loparo JJ, Takahashi M, Richardson CC, van Oijen AM. 2009. Dynamics of DNA replication loops reveal temporal control of lagging-strand synthesis. Nature 457:336-39
    • (2009) Nature , vol.457 , pp. 336-339
    • Hamdan, S.M.1    Loparo, J.J.2    Takahashi, M.3    Richardson, C.C.4    Van Oijen, A.M.5
  • 51
    • 37849031538 scopus 로고    scopus 로고
    • Dynamic disorder and stepwise deactivation in a chymotrypsin catalyzed hydrolysis reaction
    • De Cremer G, Roeffaers MB, Baruah M, Sliwa M, Sels BF, et al. 2007. Dynamic disorder and stepwise deactivation in a chymotrypsin catalyzed hydrolysis reaction. J. Am. Chem. Soc. 129:15458-59
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 15458-15459
    • De Cremer, G.1    Roeffaers, M.B.2    Baruah, M.3    Sliwa, M.4    Sels, B.F.5
  • 52
    • 0031251298 scopus 로고    scopus 로고
    • Entrapment of biocatalysts in hydrophobic sol-gel materials for use in organic chemistry
    • ReetzMT. 1997. Entrapment of biocatalysts in hydrophobic sol-gel materials for use in organic chemistry. Adv. Mater. 9:943-54
    • (1997) Adv. Mater. , vol.9 , pp. 943-954
    • Reetz, M.T.1
  • 54
    • 22244467998 scopus 로고    scopus 로고
    • Single-molecule enzymology of chymotrypsin using water-in-oil emulsion
    • Lee AI, Brody JP. 2005. Single-molecule enzymology of chymotrypsin using water-in-oil emulsion. Biophys. J. 88:4303-11
    • (2005) Biophys. J. , vol.88 , pp. 4303-4311
    • Lee, A.I.1    Brody, J.P.2
  • 55
    • 0007042628 scopus 로고    scopus 로고
    • Monitoring the Reactions of Single Enzyme Molecules and Single Metal Ions
    • Tan WH, Yeung ES. 1997. Monitoring the reactions of single enzyme molecules and single metal ions. Anal. Chem. 69:4242-48 (Pubitemid 127492530)
    • (1997) Analytical Chemistry , vol.69 , Issue.20 , pp. 4242-4248
    • Tant, W.1    Yeung, E.S.2
  • 56
    • 35448981947 scopus 로고    scopus 로고
    • Stochastic inhibitor release and binding from single-enzyme molecules
    • USA
    • Gorris HH, Rissin DM, Walt DR. 2007. Stochastic inhibitor release and binding from single-enzyme molecules. Proc. Natl. Acad. Sci. USA 104:17680-85
    • (2007) Proc. Natl. Acad. Sci. , vol.104 , pp. 17680-17685
    • Gorris, H.H.1    Rissin, D.M.2    Walt, D.R.3
  • 57
    • 69949143453 scopus 로고    scopus 로고
    • Mechanistic aspects of horseradish peroxidase elucidated through singlemolecule studies
    • Gorris HH, Walt DR. 2009. Mechanistic aspects of horseradish peroxidase elucidated through singlemolecule studies. J. Am. Chem. Soc. 131:6277-82
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 6277-6282
    • Gorris, H.H.1    Walt, D.R.2
  • 58
    • 0028934277 scopus 로고
    • Differences in the chemical reactivity of individual molecules of an enzyme
    • Xue Q, Yeung ES. 1995. Differences in the chemical reactivity of individual molecules of an enzyme. Nature 373:681-83
    • (1995) Nature , vol.373 , pp. 681-683
    • Xue, Q.1    Yeung, E.S.2
  • 59
    • 0030003076 scopus 로고    scopus 로고
    • Studies on single alkaline phosphatase molecules: Reaction rate and activation energy of a reaction catalyzed by a single molecule and the effect of thermal denaturation - The death of an enzyme
    • DOI 10.1021/ja9540839
    • Craig DB, Arriaga EA, Wong JCY, Lu H, Dovichi NJ. 1996. Studies on single alkaline phosphatase molecules: reaction rate and activation energy of a reaction catalyzed by a single molecule and the effect of thermal denaturation-the death of an enzyme. J. Am. Chem. Soc. 118:5245-53 (Pubitemid 26201544)
    • (1996) Journal of the American Chemical Society , vol.118 , Issue.22 , pp. 5245-5253
    • Craig, D.B.1    Arriaga, E.A.2    Wong, J.C.Y.3    Lu, H.4    Dovichi, N.J.5
  • 60
    • 12244291015 scopus 로고    scopus 로고
    • Crystallization of ß- galactosidase does not reduce the range of activity of individual molecules
    • Shoemaker GK, Juers DH, Coombs JM, Matthews BW, Craig DB. 2003. Crystallization of ß- galactosidase does not reduce the range of activity of individual molecules. Biochemistry 42:1707-10
    • (2003) Biochemistry , vol.42 , pp. 1707-1710
    • Shoemaker, G.K.1    Juers, D.H.2    Coombs, J.M.3    Matthews, B.W.4    Craig, D.B.5
  • 61
    • 59249087735 scopus 로고    scopus 로고
    • Continuous flow assay for the simultaneous measurement of the electrophoretic mobility catalytic activity and its variation over time of individual molecules of escherichia coli ß-galactosidase
    • Craig DB, Nichols ER. 2008. Continuous flow assay for the simultaneous measurement of the electrophoretic mobility, catalytic activity and its variation over time of individual molecules of Escherichia coli ß-galactosidase. Electrophoresis 29:4298-303
    • (2008) Electrophoresis , vol.29 , pp. 4298-4303
    • Craig, D.B.1    Nichols, E.R.2
  • 63
    • 72949103270 scopus 로고    scopus 로고
    • The potential of microfluidicwater-in-oil droplets in experimental biology
    • Schaerli Y, Hollfelder F. 2009. The potential of microfluidicwater-in-oil droplets in experimental biology. Mol. BioSyst. 5:1392-404
    • (2009) Mol. BioSyst. , vol.5 , pp. 1392-1404
    • Schaerli, Y.1    Hollfelder, F.2
  • 64
    • 60649106614 scopus 로고    scopus 로고
    • Static microdroplet arrays: A microfluidic device for droplet trapping incubation and release for enzymatic and cell-based assays
    • Huebner A, Bratton D, Whyte G, Yang M, Demello AJ, et al. 2009. Static microdroplet arrays: a microfluidic device for droplet trapping, incubation and release for enzymatic and cell-based assays. Lab Chip 9:692-98
    • (2009) Lab. Chip. , vol.9 , pp. 692-698
    • Huebner, A.1    Bratton, D.2    Whyte, G.3    Yang, M.4    Demello, A.J.5
  • 65
    • 44249106644 scopus 로고    scopus 로고
    • Green fluorescent protein in inertially injected aqueous nanodroplets
    • Tang J, Jofre AM, Lowman GM, Kishore RB, Reiner JE, et al. 2008. Green fluorescent protein in inertially injected aqueous nanodroplets. Langmuir 24:4975-78
    • (2008) Langmuir , vol.24 , pp. 4975-4978
    • Tang, J.1    Jofre, A.M.2    Lowman, G.M.3    Kishore, R.B.4    Reiner, J.E.5
  • 66
    • 12344282980 scopus 로고    scopus 로고
    • Detection of intensity change points in time-resolved single-molecule measurements
    • DOI 10.1021/jp0467548
    • Watkins LP, Yang H. 2005. Detection of intensity change points in time-resolved single-molecule measurements. J. Phys. Chem. B 109:617-28 (Pubitemid 40121008)
    • (2005) Journal of Physical Chemistry B , vol.109 , Issue.1 , pp. 617-628
    • Watkins, L.P.1    Yang, H.2
  • 67
    • 33847300137 scopus 로고    scopus 로고
    • Multiscale change point analysis in Poisson count data
    • DOI 10.1016/j.chemolab.2006.05.014, PII S016974390600133X
    • Jansen M. 2007. Multiscale change point analysis in Poisson count data. Chemom. Intell. Lab. Syst. 85:159-69 (Pubitemid 46329191)
    • (2007) Chemometrics and Intelligent Laboratory Systems , vol.85 , Issue.2 , pp. 159-169
    • Jansen, M.1
  • 69
    • 7044253170 scopus 로고    scopus 로고
    • Single molecule kinetics I theoretical analysis of indicators
    • Witkoskie JB, Cao J. 2004. Single molecule kinetics. I. Theoretical analysis of indicators. J. Chem. Phys. 121:6361-72
    • (2004) J. Chem. Phys. , vol.121 , pp. 6361-6372
    • Witkoskie, J.B.1    Cao, J.2
  • 70
    • 22244469413 scopus 로고    scopus 로고
    • What can one learn from two-state single-molecule trajectories?
    • DOI 10.1529/biophysj.104.055905
    • Flomenbom O, Klafter J, Szabo A. 2005. What can one learn from two-state single-molecule trajectories? Biophys. J. 88:3780-83 (Pubitemid 40991093)
    • (2005) Biophysical Journal , vol.88 , Issue.6 , pp. 3780-3783
    • Flomenbom, O.1    Klafter, J.2    Szabo, A.3
  • 71
    • 35448958522 scopus 로고    scopus 로고
    • Markov processes in single molecule fluorescence
    • Talaga DS. 2007. Markov processes in single molecule fluorescence. Curr. Opin. Colloid Interface Sci. 12:285-96
    • (2007) Curr. Opin. Colloid Interface Sci. , vol.12 , pp. 285-296
    • Talaga, D.S.1
  • 73
    • 33845360042 scopus 로고    scopus 로고
    • Ultra-high resolution imaging by fluorescence photoactivation localization microscopy
    • Hess ST, Girirajan TPK, Mason MD. 2006. Ultra-high resolution imaging by fluorescence photoactivation localization microscopy. Biophys. J. 91:4258-72
    • (2006) Biophys. J. , vol.91 , pp. 4258-4272
    • Hess, S.T.1    Girirajan, T.P.K.2    Mason, M.D.3
  • 74
    • 33749026335 scopus 로고    scopus 로고
    • Sub-diffraction-limit imaging by stochastic optical reconstruction microscopy (STORM)
    • DOI 10.1038/nmeth929, PII NMETH929
    • Rust MJ, Bates M, Zhuang XW. 2006. Sub-diffraction-limit imaging by stochastic optical reconstruction microscopy (STORM). Nat. Methods 3:793-95 (Pubitemid 44445825)
    • (2006) Nature Methods , vol.3 , Issue.10 , pp. 793-795
    • Rust, M.J.1    Bates, M.2    Zhuang, X.3
  • 78
    • 42949083695 scopus 로고    scopus 로고
    • Live-cell photoactivated localization microscopy of nanoscale adhesion dynamics
    • DOI 10.1038/nmeth.1202, PII NMETH.1202
    • Shroff H, Galbraith CG, Galbraith JA, Betzig E. 2008. Live-cell photoactivated localization microscopy of nanoscale adhesion dynamics. Nat. Methods 5:417-23 (Pubitemid 351619100)
    • (2008) Nature Methods , vol.5 , Issue.5 , pp. 417-423
    • Shroff, H.1    Galbraith, C.G.2    Galbraith, J.A.3    Betzig, E.4
  • 80
    • 0025342635 scopus 로고
    • Two-photon laser scanning fluorescence microscopy
    • Denk W, Strickler JH, Webb WW. 1990. Two-photon laser scanning fluorescence microscopy. Science 248:73-76 (Pubitemid 20139273)
    • (1990) Science , vol.248 , Issue.4951 , pp. 73-76
    • Denk, W.1    Strickler, J.H.2    Webb, W.W.3


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