메뉴 건너뛰기




Volumn 1657, Issue 2-3, 2004, Pages 82-104

Erratum: Global and target analysis of time-resolved spectra (Biochimica et Biophysica Acta (2004) 1658: 2-3 (82-104) PII: S0005-2728(04)00109-4 and DOI: 10.1016/j.bbabio.2004.04.011);Global and target analysis of time-resolved spectra

Author keywords

bacteriorhodopsin; BR; DADS; DAS; Decay Associated Difference Spectra; Decay Associated Spectra; EADS; Global analysis; Multiway data; Photoactive yellow protein; Spectrotemporal model; Target analysis; Time resolved spectroscopy

Indexed keywords

PROTEIN;

EID: 3242662628     PISSN: 00052728     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbabio.2004.08.005     Document Type: Erratum
Times cited : (1443)

References (106)
  • 1
    • 0028950771 scopus 로고
    • Time-resolved fluorescence spectroscopy
    • Holzwarth A.R. Time-resolved fluorescence spectroscopy. Methods Enzymol. 246:1995;334-362
    • (1995) Methods Enzymol. , vol.246 , pp. 334-362
    • Holzwarth, A.R.1
  • 2
    • 0028929508 scopus 로고
    • Transient absorption spectroscopy in study of processes and dynamics in biology
    • van Amerongen H., van Grondelle R. Transient absorption spectroscopy in study of processes and dynamics in biology. Methods Enzymol. 246:1995;201-226
    • (1995) Methods Enzymol. , vol.246 , pp. 201-226
    • Van Amerongen, H.1    Van Grondelle, R.2
  • 3
    • 0016723355 scopus 로고
    • Bacteriorhodopsin: A light-driven proton pump in Halobacterium halobium
    • Lozier R.H., Bogomolni R.A., Stoeckenius W. Bacteriorhodopsin: a light-driven proton pump in Halobacterium halobium. Biophys. J. 15:1975;955-962
    • (1975) Biophys. J. , vol.15 , pp. 955-962
    • Lozier, R.H.1    Bogomolni, R.A.2    Stoeckenius, W.3
  • 4
    • 0002979180 scopus 로고
    • Light energy transduction in bacteriorhodopsin
    • M.B. Jackson. Boca Raton, FL: CRC. Chap. 10
    • Ebrey T.G. Light energy transduction in bacteriorhodopsin. Jackson M.B. Thermodynamics of Membrane Receptors and Channels. 1993;CRC, Boca Raton, FL. Chap. 10
    • (1993) Thermodynamics of Membrane Receptors and Channels
    • Ebrey, T.G.1
  • 5
    • 0023152468 scopus 로고
    • Properties of a water-soluble, yellow protein isolated from a halophilic phototrophic bacterium that has photochemical activity analogous to sensory rhodopsin
    • Meyer T.E., Yakali E., Cusanovich M.A., Tollin G. Properties of a water-soluble, yellow protein isolated from a halophilic phototrophic bacterium that has photochemical activity analogous to sensory rhodopsin. Biochemistry. 26:1987;418-423
    • (1987) Biochemistry , vol.26 , pp. 418-423
    • Meyer, T.E.1    Yakali, E.2    Cusanovich, M.A.3    Tollin, G.4
  • 6
    • 0037468225 scopus 로고    scopus 로고
    • Photoactive Yellow Protein, a new type of photoreceptor protein: Will this "yellow lab" bring us where we want to go?
    • Hellingwerf K.J., Hendriks J., Gensch T. Photoactive Yellow Protein, a new type of photoreceptor protein: will this "yellow lab" bring us where we want to go? J. Phys. Chem., A. 107:2003;1082-1094
    • (2003) J. Phys. Chem., a , vol.107 , pp. 1082-1094
    • Hellingwerf, K.J.1    Hendriks, J.2    Gensch, T.3
  • 9
    • 0001304864 scopus 로고    scopus 로고
    • Review of chemometrics applied to spectroscopy: 1985-95: 3. Multi-way analysis
    • Bro R., Workman J.J., Mobley P.R., Kowalski B.R. Review of chemometrics applied to spectroscopy: 1985-95: 3. Multi-way analysis. Appl. Spectrosc. Rev. 32:1997;237-261
    • (1997) Appl. Spectrosc. Rev. , vol.32 , pp. 237-261
    • Bro, R.1    Workman, J.J.2    Mobley, P.R.3    Kowalski, B.R.4
  • 10
    • 0033661648 scopus 로고    scopus 로고
    • Estimating reaction rate constants from a two-step reaction: A comparison between two-way and three-way methods
    • Bijlsma S., Smilde A.K. Estimating reaction rate constants from a two-step reaction: a comparison between two-way and three-way methods. J. Chemom. 14:2000;541-560
    • (2000) J. Chemom. , vol.14 , pp. 541-560
    • Bijlsma, S.1    Smilde, A.K.2
  • 11
    • 0022124249 scopus 로고
    • Global and target analysis of complex decay phenomena
    • Beechem J.M., Ameloot M., Brand L. Global and target analysis of complex decay phenomena. Anal. Instrum. 14:1985;379-402
    • (1985) Anal. Instrum. , vol.14 , pp. 379-402
    • Beechem, J.M.1    Ameloot, M.2    Brand, L.3
  • 12
    • 0024676128 scopus 로고
    • A second generation global analysis program for the recovery of complex inhomogeneous fluorescence decay kinetics
    • Beechem J.M. A second generation global analysis program for the recovery of complex inhomogeneous fluorescence decay kinetics. Chem. Phys. Lipids. 50:1989;237-251
    • (1989) Chem. Phys. Lipids , vol.50 , pp. 237-251
    • Beechem, J.M.1
  • 13
    • 0026719686 scopus 로고
    • Global analysis program of biochemical and biophysical data
    • Beechem J.M. Global analysis program of biochemical and biophysical data. Methods Enzymol. 210:1992;37-54
    • (1992) Methods Enzymol. , vol.210 , pp. 37-54
    • Beechem, J.M.1
  • 15
    • 0002272436 scopus 로고    scopus 로고
    • Data analysis of time-resolved measurements
    • J. Amesz, & A.J. Hoff. Dordrecht, the Netherlands: Kluwer Academic Publishing
    • Holzwarth A.R. Data analysis of time-resolved measurements. Amesz J., Hoff A.J. Biophysical Techniques in Photosynthesis. 1996;75-92 Kluwer Academic Publishing, Dordrecht, the Netherlands
    • (1996) Biophysical Techniques in Photosynthesis , pp. 75-92
    • Holzwarth, A.R.1
  • 16
    • 0030728340 scopus 로고    scopus 로고
    • Evaluation of intrinsic chemical kinetics and transient product spectra from time-resolved spectroscopic data
    • Dioumaev A.K. Evaluation of intrinsic chemical kinetics and transient product spectra from time-resolved spectroscopic data. Biophys. Chem. 67:1997;1-25
    • (1997) Biophys. Chem. , vol.67 , pp. 1-25
    • Dioumaev, A.K.1
  • 17
    • 0642281492 scopus 로고    scopus 로고
    • Methods for the analysis of transient absorbance data
    • Bonneau R., Wirz J., Zuberbühler A.D. Methods for the analysis of transient absorbance data. Pure Appl. Chem. 69:1997;979-992
    • (1997) Pure Appl. Chem. , vol.69 , pp. 979-992
    • Bonneau, R.1    Wirz, J.2    Zuberbühler, A.D.3
  • 18
    • 0020133090 scopus 로고
    • Procedure for testing kinetic models of the photocycle of bacteriorhodopsin
    • Nagle J.F., Parodi L.A., Lozier R.H. Procedure for testing kinetic models of the photocycle of bacteriorhodopsin. Biophys. J. 38:1982;161-174
    • (1982) Biophys. J. , vol.38 , pp. 161-174
    • Nagle, J.F.1    Parodi, L.A.2    Lozier, R.H.3
  • 19
    • 0026092691 scopus 로고
    • Solving complex photocycle kinetics. Theory and direct method
    • Nagle J.F. Solving complex photocycle kinetics. Theory and direct method. Biophys. J. 59:1991;476-487
    • (1991) Biophys. J. , vol.59 , pp. 476-487
    • Nagle, J.F.1
  • 21
    • 0035953964 scopus 로고    scopus 로고
    • Theory and procedures for finding a correct kinetic model for the bacteriorhodopsin photocycle
    • Hendler R.W., Shrager R.I., Bose S. Theory and procedures for finding a correct kinetic model for the bacteriorhodopsin photocycle. J. Phys. Chem., B. 105:2001;3319-3328
    • (2001) J. Phys. Chem., B. , vol.105 , pp. 3319-3328
    • Hendler, R.W.1    Shrager, R.I.2    Bose, S.3
  • 22
    • 0037456295 scopus 로고    scopus 로고
    • Critical evaluation of kinetic models for bacteriorhodopsin photocycles
    • Shrager R.I., Hendler R.W. Critical evaluation of kinetic models for bacteriorhodopsin photocycles. J. Phys. Chem., B. 107:2003;1708-1713
    • (2003) J. Phys. Chem., B. , vol.107 , pp. 1708-1713
    • Shrager, R.I.1    Hendler, R.W.2
  • 23
    • 0037018561 scopus 로고    scopus 로고
    • Target analysis of the bacteriorhodopsin photocycle using a spectrotemporal model
    • van Stokkum I.H.M., Lozier R.H. Target analysis of the bacteriorhodopsin photocycle using a spectrotemporal model. J. Phys. Chem., B. 106:2002;3477-3485
    • (2002) J. Phys. Chem., B , vol.106 , pp. 3477-3485
    • Van Stokkum, I.H.M.1    Lozier, R.H.2
  • 27
    • 0343853850 scopus 로고
    • Picosecond time-resolved absorption spectrometer using a streak camera
    • Ito T., Hiramatsu M., Hosoda M., Tsuchiya Y. Picosecond time-resolved absorption spectrometer using a streak camera. Rev. Sci. Instrum. 62:1991;1415-1419
    • (1991) Rev. Sci. Instrum. , vol.62 , pp. 1415-1419
    • Ito, T.1    Hiramatsu, M.2    Hosoda, M.3    Tsuchiya, Y.4
  • 28
    • 0000891284 scopus 로고
    • Possibilities and limitations of the time-correlated single photon counting technique: A comparative study of correction methods for the wavelength dependence of the instrument response function
    • van den Zegel M., Boens N., Daems D., de Schryver F.C. Possibilities and limitations of the time-correlated single photon counting technique: a comparative study of correction methods for the wavelength dependence of the instrument response function. Chem. Phys. 101:1986;311-335
    • (1986) Chem. Phys. , vol.101 , pp. 311-335
    • Van Den Zegel, M.1    Boens, N.2    Daems, D.3    De Schryver, F.C.4
  • 29
    • 84989691716 scopus 로고
    • Picosecond single photon timing measurements with a proximity type microchannel plate photomultiplier and global analysis with reference convolution
    • Boens N., Tamai N., Yamazaki I., Yamazaki T. Picosecond single photon timing measurements with a proximity type microchannel plate photomultiplier and global analysis with reference convolution. Photochem. Photobiol. 52:1990;911-917
    • (1990) Photochem. Photobiol. , vol.52 , pp. 911-917
    • Boens, N.1    Tamai, N.2    Yamazaki, I.3    Yamazaki, T.4
  • 31
    • 0033089462 scopus 로고    scopus 로고
    • Femtosecond spectroscopy of condensed phases with chirped supercontinuum probing
    • Kovalenko S.A., Dobryakov A.L., Ruthmann J., Ernsting N.P. Femtosecond spectroscopy of condensed phases with chirped supercontinuum probing. Phys. Rev., A. 59:1999;2369-2384
    • (1999) Phys. Rev., a , vol.59 , pp. 2369-2384
    • Kovalenko, S.A.1    Dobryakov, A.L.2    Ruthmann, J.3    Ernsting, N.P.4
  • 32
    • 0000501547 scopus 로고
    • Multiresponse parameter estimation and compartmental analysis of time resolved fluorescence spectra. Application to conformational dynamics of charge-separated species in solution
    • van Stokkum I.H.M., Brouwer A.M., van Ramesdonk H.J., Scherer T. Multiresponse parameter estimation and compartmental analysis of time resolved fluorescence spectra. Application to conformational dynamics of charge-separated species in solution. Proc. K. Ned. Akad. v. Wet. 96:1993;43-68
    • (1993) Proc. K. Ned. Akad. V. Wet. , vol.96 , pp. 43-68
    • Van Stokkum, I.H.M.1    Brouwer, A.M.2    Van Ramesdonk, H.J.3    Scherer, T.4
  • 33
    • 0003558340 scopus 로고
    • Applied Linear Regression
    • New York: Wiley
    • Weisberg S. Applied Linear Regression. 2nd ed.:1985;Wiley, New York
    • (1985) 2nd Ed.
    • Weisberg, S.1
  • 34
    • 0026083378 scopus 로고
    • Variance reduction by simultaneous multi-exponential analysis of data sets from different experiments
    • Müller K.-H., Plesser Th. Variance reduction by simultaneous multi-exponential analysis of data sets from different experiments. Eur. Biophys. J. 19:1991;231-240
    • (1991) Eur. Biophys. J. , vol.19 , pp. 231-240
    • Müller, K.-H.1    Plesser, Th.2
  • 35
    • 0004165224 scopus 로고
    • Chemical Kinetics
    • New York: Harper and Row
    • Laidler K.J. Chemical Kinetics. 3rd ed.:1987;Harper and Row, New York
    • (1987) 3rd Ed.
    • Laidler, K.J.1
  • 36
    • 0041839407 scopus 로고    scopus 로고
    • Femtosecond chemical dynamics in condensed phases
    • Fleming G.R., Joo T., Cho M. Femtosecond chemical dynamics in condensed phases. Adv. Chem. Phys. 101:1997;141-183
    • (1997) Adv. Chem. Phys. , vol.101 , pp. 141-183
    • Fleming, G.R.1    Joo, T.2    Cho, M.3
  • 37
    • 0026710549 scopus 로고
    • Global target analysis of picosecond chlorophyll fluorescence kinetics from pea chloroplasts. a new approach to the characterization of the primary processes in photosystem II α- And β-units
    • Roelofs T.A., Lee C.H., Holzwarth A.R. Global target analysis of picosecond chlorophyll fluorescence kinetics from pea chloroplasts. A new approach to the characterization of the primary processes in photosystem II α- and β-units. Biophys. J. 61:1992;1147-1163
    • (1992) Biophys. J. , vol.61 , pp. 1147-1163
    • Roelofs, T.A.1    Lee, C.H.2    Holzwarth, A.R.3
  • 38
    • 0020176542 scopus 로고
    • A constrained regularization method for inverting data represented by linear algebraic or integral equations
    • Provencher S.W. A constrained regularization method for inverting data represented by linear algebraic or integral equations. Comp. Phys. Commun. 27:1982;213-227
    • (1982) Comp. Phys. Commun. , vol.27 , pp. 213-227
    • Provencher, S.W.1
  • 39
    • 0028672799 scopus 로고
    • Maximum-entropy method of data-analysis in time-resolved spectroscopy
    • Brochon J.C. Maximum-entropy method of data-analysis in time-resolved spectroscopy. Methods Enzymol. 240:1994;262-311
    • (1994) Methods Enzymol. , vol.240 , pp. 262-311
    • Brochon, J.C.1
  • 41
    • 84886363141 scopus 로고
    • Mixture analysis using factor analysis: II. Self modeling curve resolution
    • Hamilton J.C., Gemperline P.J. Mixture analysis using factor analysis: II. Self modeling curve resolution. J. Chemom. 4:1990;1-13
    • (1990) J. Chemom. , vol.4 , pp. 1-13
    • Hamilton, J.C.1    Gemperline, P.J.2
  • 42
    • 0026675184 scopus 로고
    • Self-modeling mixture analysis of spectral data with continuous concentration profiles
    • Windig W. Self-modeling mixture analysis of spectral data with continuous concentration profiles. Chemom. Intell. Lab. Syst. 16:1992;1-16
    • (1992) Chemom. Intell. Lab. Syst. , vol.16 , pp. 1-16
    • Windig, W.1
  • 43
    • 0033551157 scopus 로고    scopus 로고
    • Singular value decomposition with self-modeling applied to determine bacteriorhodopsin intermediate spectra: Analysis of simulated data
    • Zimányi L., Kulcsár A., Lanyi J.K., Sears D.F., Saltiel J. Singular value decomposition with self-modeling applied to determine bacteriorhodopsin intermediate spectra: analysis of simulated data. Proc. Natl. Acad. Sci. U. S. A. 96:1999;4408-4413
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 4408-4413
    • Zimányi, L.1    Kulcsár, A.2    Lanyi, J.K.3    Sears, D.F.4    Saltiel, J.5
  • 44
    • 0033551253 scopus 로고    scopus 로고
    • Intermediate spectra and photocycle kinetics of the Asp96→Asn mutant bacteriorhodopsin determined by singular value decomposition with self-modeling
    • Zimányi L., Kulcsár A., Lanyi J.K., Sears D.F., Saltiel J. Intermediate spectra and photocycle kinetics of the Asp96→Asn mutant bacteriorhodopsin determined by singular value decomposition with self-modeling. Proc. Natl. Acad. Sci. U. S. A. 96:1999;4414-4419
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 4414-4419
    • Zimányi, L.1    Kulcsár, A.2    Lanyi, J.K.3    Sears, D.F.4    Saltiel, J.5
  • 45
    • 0034836294 scopus 로고    scopus 로고
    • Dissecting the photocycle of the bacteriorhodopsin E204Q mutant from kinetic multichannel difference spectra. Extension of the method of singular value decomposition with self-modeling to five components
    • Kulcsár A., Saltiel J., Zimányi L. Dissecting the photocycle of the bacteriorhodopsin E204Q mutant from kinetic multichannel difference spectra. Extension of the method of singular value decomposition with self-modeling to five components. J. Am. Chem. Soc. 123:2001;3332-3340
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 3332-3340
    • Kulcsár, A.1    Saltiel, J.2    Zimányi, L.3
  • 46
    • 0020338868 scopus 로고
    • A pulse radiolysis-computer simulation method for resolving of complex kinetics and spectra
    • Solar S., Solar W., Getoff N. A pulse radiolysis-computer simulation method for resolving of complex kinetics and spectra. Radiat. Phys. Chem. 21:1983;129-138
    • (1983) Radiat. Phys. Chem. , vol.21 , pp. 129-138
    • Solar, S.1    Solar, W.2    Getoff, N.3
  • 47
    • 0023863439 scopus 로고
    • Spectral and kinetic properties of intermediates induced by reaction of hydrated electrons with adenine, adenosine, adenylic acid and polyadenylic acid; A multi component analysis
    • Visscher K.J., Hom M.L., Loman H., Spoelder H.J.W., Verberne J.B. Spectral and kinetic properties of intermediates induced by reaction of hydrated electrons with adenine, adenosine, adenylic acid and polyadenylic acid; a multi component analysis. Radiat. Phys. Chem. 32:1988;465-473
    • (1988) Radiat. Phys. Chem. , vol.32 , pp. 465-473
    • Visscher, K.J.1    Hom, M.L.2    Loman, H.3    Spoelder, H.J.W.4    Verberne, J.B.5
  • 48
    • 0019527620 scopus 로고
    • Resolution of multicomponent fluorescence spectra by an emission wavelength-decay time data matrix
    • Knorr F.J., Harris J.M. Resolution of multicomponent fluorescence spectra by an emission wavelength-decay time data matrix. Anal. Chem. 53:1981;272-276
    • (1981) Anal. Chem. , vol.53 , pp. 272-276
    • Knorr, F.J.1    Harris, J.M.2
  • 49
    • 0000276506 scopus 로고
    • Global analysis of fluorescence decay surfaces: Excited-state reactions
    • Beechem J.M., Ameloot M., Brand L. Global analysis of fluorescence decay surfaces: excited-state reactions. Chem. Phys. Lett. 120:1985;466-472
    • (1985) Chem. Phys. Lett. , vol.120 , pp. 466-472
    • Beechem, J.M.1    Ameloot, M.2    Brand, L.3
  • 50
    • 0000060559 scopus 로고
    • Simultaneous analysis of multiple fluorescence decay curves: A global approach
    • Knutson J.R., Beechem J.M., Brand L. Simultaneous analysis of multiple fluorescence decay curves: a global approach. Chem. Phys. Lett. 102:1983;501-507
    • (1983) Chem. Phys. Lett. , vol.102 , pp. 501-507
    • Knutson, J.R.1    Beechem, J.M.2    Brand, L.3
  • 51
    • 0000789205 scopus 로고
    • Time-resolved emission spectra, decay-associated spectra, and species-associated spectra
    • Löfroth J.E. Time-resolved emission spectra, decay-associated spectra, and species-associated spectra. J. Phys. Chem. 90:1986;1160-1168
    • (1986) J. Phys. Chem. , vol.90 , pp. 1160-1168
    • Löfroth, J.E.1
  • 52
    • 0142135186 scopus 로고    scopus 로고
    • Ultrafast fluorescence relaxation spectroscopy of 6,7-dimethyl-(8- ribityl)-lumazine and riboflavin, free and bound to antenna proteins from bioluminescent bacteria
    • Petushkov V.N., van Stokkum I.H.M., Gobets B., van Mourik F., Lee J., van Grondelle R., Visser A.J.W.G. Ultrafast fluorescence relaxation spectroscopy of 6,7-dimethyl-(8-ribityl)-lumazine and riboflavin, free and bound to antenna proteins from bioluminescent bacteria. J. Phys. Chem., B. 107:2003;10934-10939
    • (2003) J. Phys. Chem., B , vol.107 , pp. 10934-10939
    • Petushkov, V.N.1    Van Stokkum, I.H.M.2    Gobets, B.3    Van Mourik, F.4    Lee, J.5    Van Grondelle, R.6    Visser, A.J.W.G.7
  • 53
    • 0035144442 scopus 로고    scopus 로고
    • Carotenoid-to-chlorophyll energy transfer in recombinant major light-harvesting complex (LHCII) of higher plants: I. Femtosecond transient absorption measurements
    • Croce R., Müller M.G., Bassi R., Holzwarth A.R. Carotenoid-to- chlorophyll energy transfer in recombinant major light-harvesting complex (LHCII) of higher plants: I. Femtosecond transient absorption measurements. Biophys. J. 80:2001;901-915
    • (2001) Biophys. J. , vol.80 , pp. 901-915
    • Croce, R.1    Müller, M.G.2    Bassi, R.3    Holzwarth, A.R.4
  • 54
    • 18544404159 scopus 로고    scopus 로고
    • Ultrafast transient absorption studies on Photosystem I reaction centers from Chlamydomonas reinhardtii: 1. a new interpretation of the energy trapping and early electron transfer steps in Photosystem I
    • Müller M.G., Niklas J., Lubitz W., Holzwarth A.R. Ultrafast transient absorption studies on Photosystem I reaction centers from Chlamydomonas reinhardtii: 1. A new interpretation of the energy trapping and early electron transfer steps in Photosystem I. Biophys. J. 85:2003;3899-3922
    • (2003) Biophys. J. , vol.85 , pp. 3899-3922
    • Müller, M.G.1    Niklas, J.2    Lubitz, W.3    Holzwarth, A.R.4
  • 58
    • 0011479904 scopus 로고
    • Intensity deconvolution in fluorescence depolarization studies of liquids, liquid crystals and membranes
    • Arcioni A., Zannoni C. Intensity deconvolution in fluorescence depolarization studies of liquids, liquid crystals and membranes. Chem. Phys. 88:1984;113-128
    • (1984) Chem. Phys. , vol.88 , pp. 113-128
    • Arcioni, A.1    Zannoni, C.2
  • 59
    • 0030984493 scopus 로고    scopus 로고
    • Primary electron transfer kinetics in membrane-bound Rhodobacter sphaeroides reaction centers: A global and target analysis
    • van Stokkum I.H.M., Beekman L.M.P., Jones M.R., van Brederode M.E., van Grondelle R. Primary electron transfer kinetics in membrane-bound Rhodobacter sphaeroides reaction centers: a global and target analysis. Biochemistry. 36:1997;11360-11368
    • (1997) Biochemistry , vol.36 , pp. 11360-11368
    • Van Stokkum, I.H.M.1    Beekman, L.M.P.2    Jones, M.R.3    Van Brederode, M.E.4    Van Grondelle, R.5
  • 60
    • 0000757515 scopus 로고
    • Identifiability and distinguishability of first-order reaction systems
    • Vajda S., Rabitz H. Identifiability and distinguishability of first-order reaction systems. J. Phys. Chem. 92:1988;701-707
    • (1988) J. Phys. Chem. , vol.92 , pp. 701-707
    • Vajda, S.1    Rabitz, H.2
  • 61
    • 0018452473 scopus 로고
    • A systems-theory approach to the analysis of multiexponential fluorescence decay
    • Eisenfeld J., Ford C.C. A systems-theory approach to the analysis of multiexponential fluorescence decay. Biophys. J. 26:1979;73-84
    • (1979) Biophys. J. , vol.26 , pp. 73-84
    • Eisenfeld, J.1    Ford, C.C.2
  • 62
    • 0001302210 scopus 로고
    • Conformational dynamics of flexibly and semirigidly bridged electron donor-acceptor systems as revealed by spectrotemporal parameterization of fluorescence
    • van Stokkum I.H.M., Scherer T., Brouwer A.M., Verhoeven J.W. Conformational dynamics of flexibly and semirigidly bridged electron donor-acceptor systems as revealed by spectrotemporal parameterization of fluorescence. J. Phys. Chem. 98:1994;852-866
    • (1994) J. Phys. Chem. , vol.98 , pp. 852-866
    • Van Stokkum, I.H.M.1    Scherer, T.2    Brouwer, A.M.3    Verhoeven, J.W.4
  • 63
    • 0039461370 scopus 로고
    • Primary processes in isolated bacterial reaction centers from Rhodobacter sphaeroides studied by picosecond fluorescence kinetics
    • Müller M.G., Griebenow K., Holzwarth A.R. Primary processes in isolated bacterial reaction centers from Rhodobacter sphaeroides studied by picosecond fluorescence kinetics. Chem. Phys. Lett. 199:1992;465-469
    • (1992) Chem. Phys. Lett. , vol.199 , pp. 465-469
    • Müller, M.G.1    Griebenow, K.2    Holzwarth, A.R.3
  • 66
    • 0029148319 scopus 로고
    • Temperature-induced changes in protein structures studied by Fourier transform infrared spectroscopy and global analysis
    • van Stokkum I.H.M., Linsdell H., Hadden J.M., Haris P.I., Chapman D., Bloemendal M. Temperature-induced changes in protein structures studied by Fourier transform infrared spectroscopy and global analysis. Biochemistry. 34:1995;10508-10518
    • (1995) Biochemistry , vol.34 , pp. 10508-10518
    • Van Stokkum, I.H.M.1    Linsdell, H.2    Hadden, J.M.3    Haris, P.I.4    Chapman, D.5    Bloemendal, M.6
  • 67
    • 84949218859 scopus 로고
    • A stochastic theory of lineshape
    • Kubo R. A stochastic theory of lineshape. Adv. Chem. Phys. 15:1969;101-127
    • (1969) Adv. Chem. Phys. , vol.15 , pp. 101-127
    • Kubo, R.1
  • 68
    • 0346198884 scopus 로고
    • Relation between charge transfer absorption and fluorescence spectra and the inverted region
    • Marcus R.A. Relation between charge transfer absorption and fluorescence spectra and the inverted region. J. Phys. Chem. 93:1989;3078-3086
    • (1989) J. Phys. Chem. , vol.93 , pp. 3078-3086
    • Marcus, R.A.1
  • 70
    • 0002419950 scopus 로고
    • Resolution of overlapping bands: Functions for simulating band shapes
    • Fraser R.D.B., Suzuki E. Resolution of overlapping bands: functions for simulating band shapes. Anal. Chem. 41:1969;37-39
    • (1969) Anal. Chem. , vol.41 , pp. 37-39
    • Fraser, R.D.B.1    Suzuki, E.2
  • 72
    • 21844484331 scopus 로고
    • Temperature dependence of electron-vibronic spectra of photosynthetic systems. Computer simulations and comparison with experiment
    • Pullerits T., Monshouwer R., van Mourik F., van Grondelle R. Temperature dependence of electron-vibronic spectra of photosynthetic systems. Computer simulations and comparison with experiment. Chem. Phys. 194:1995;395-407
    • (1995) Chem. Phys. , vol.194 , pp. 395-407
    • Pullerits, T.1    Monshouwer, R.2    Van Mourik, F.3    Van Grondelle, R.4
  • 74
    • 33845555570 scopus 로고
    • Titration of individual components in a mixture with resolution of difference spectra, pKs, and redox transitions
    • Shrager R.I., Hendler R.W. Titration of individual components in a mixture with resolution of difference spectra, pKs, and redox transitions. Anal. Chem. 54:1982;1147-1152
    • (1982) Anal. Chem. , vol.54 , pp. 1147-1152
    • Shrager, R.I.1    Hendler, R.W.2
  • 75
    • 0003076541 scopus 로고
    • Chemical transitions measured by spectra and resolved using singular value decomposition
    • Shrager R.I. Chemical transitions measured by spectra and resolved using singular value decomposition. Chemom. Intell. Lab. Syst. 1:1986;59-70
    • (1986) Chemom. Intell. Lab. Syst. , vol.1 , pp. 59-70
    • Shrager, R.I.1
  • 76
    • 0026633609 scopus 로고
    • Singular value decomposition: Application to analysis of experimental data
    • Henry E.R., Hofrichter J. Singular value decomposition: application to analysis of experimental data. Methods Enzymol. 210:1992;129-192
    • (1992) Methods Enzymol. , vol.210 , pp. 129-192
    • Henry, E.R.1    Hofrichter, J.2
  • 77
    • 0027976593 scopus 로고
    • Deconvolutions based on singular-value decomposition and the pseudoinverse - A guide for beginners
    • Hendler R.W., Shrager R.I. Deconvolutions based on singular-value decomposition and the pseudoinverse - a guide for beginners. J. Biochem. Biophys. Methods. 28:1994;1-33
    • (1994) J. Biochem. Biophys. Methods , vol.28 , pp. 1-33
    • Hendler, R.W.1    Shrager, R.I.2
  • 78
    • 0031013417 scopus 로고    scopus 로고
    • The use of matrix methods in the modeling of spectroscopic data sets
    • Henry E.R. The use of matrix methods in the modeling of spectroscopic data sets. Biophys. J. 72:1997;652-673
    • (1997) Biophys. J. , vol.72 , pp. 652-673
    • Henry, E.R.1
  • 79
    • 1042278933 scopus 로고    scopus 로고
    • Visualization of transient absorption dynamics - Towards a qualitative view of complex reaction kinetics
    • Satzger H., Zinth W. Visualization of transient absorption dynamics - towards a qualitative view of complex reaction kinetics. Chem. Phys. 295:2003;287-295
    • (2003) Chem. Phys. , vol.295 , pp. 287-295
    • Satzger, H.1    Zinth, W.2
  • 80
    • 0026274895 scopus 로고
    • Photocycle kinetics: Analysis of Raman data from bacteriorhodopsin
    • Nagle J.F. Photocycle kinetics: analysis of Raman data from bacteriorhodopsin. Photochem. Photobiol. 54:1991;897-903
    • (1991) Photochem. Photobiol. , vol.54 , pp. 897-903
    • Nagle, J.F.1
  • 81
    • 0030749599 scopus 로고    scopus 로고
    • Deriving reaction mechanisms from kinetic spectroscopy. Application to late rhodopsin intermediates
    • Szundi I., Lewis J.W., Kliger D.S. Deriving reaction mechanisms from kinetic spectroscopy. Application to late rhodopsin intermediates. Biophys. J. 73:1997;688-702
    • (1997) Biophys. J. , vol.73 , pp. 688-702
    • Szundi, I.1    Lewis, J.W.2    Kliger, D.S.3
  • 82
    • 0029063318 scopus 로고
    • An introduction to tensor-products with applications to multiway data-analysis
    • Burdick D.S. An introduction to tensor-products with applications to multiway data-analysis. Chemom. Intell. Lab. Syst. 28:1995;229-237
    • (1995) Chemom. Intell. Lab. Syst. , vol.28 , pp. 229-237
    • Burdick, D.S.1
  • 83
    • 0035918547 scopus 로고    scopus 로고
    • Primary photoreaction of photoactive yellow protein studied by subpicosecond-nanosecond spectroscopy
    • Imamoto Y., Kataoka M., Tokunaga F., Asahi T., Masuhara H. Primary photoreaction of photoactive yellow protein studied by subpicosecond-nanosecond spectroscopy. Biochemistry. 40:2001;6047-6052
    • (2001) Biochemistry , vol.40 , pp. 6047-6052
    • Imamoto, Y.1    Kataoka, M.2    Tokunaga, F.3    Asahi, T.4    Masuhara, H.5
  • 84
    • 0037342350 scopus 로고    scopus 로고
    • Application of singular value decomposition to the analysis of time-resolved macromolecular X-ray data
    • Schmidt M., Rajagopal S., Ren Z., Moffat K. Application of singular value decomposition to the analysis of time-resolved macromolecular X-ray data. Biophys. J. 84:2003;2112-2129
    • (2003) Biophys. J. , vol.84 , pp. 2112-2129
    • Schmidt, M.1    Rajagopal, S.2    Ren, Z.3    Moffat, K.4
  • 85
    • 0037390670 scopus 로고    scopus 로고
    • Separable nonlinear least squares: The variable projection method and its applications
    • Golub G., Pereyra V. Separable nonlinear least squares: the variable projection method and its applications. Inverse Probl. 19:2003;R1-R26
    • (2003) Inverse Probl. , vol.19
    • Golub, G.1    Pereyra, V.2
  • 86
    • 0029403121 scopus 로고
    • Subpicosecond measurements of polar solvation dynamics: Coumarin 153 revisited
    • Horng M.L., Gardecki J.A., Papazyan A., Maroncelli M. Subpicosecond measurements of polar solvation dynamics: coumarin 153 revisited. J. Phys. Chem. 99:1995;17311-17337
    • (1995) J. Phys. Chem. , vol.99 , pp. 17311-17337
    • Horng, M.L.1    Gardecki, J.A.2    Papazyan, A.3    Maroncelli, M.4
  • 87
    • 0035868920 scopus 로고    scopus 로고
    • Map for the relaxation dynamics of hot photoelectrons injected into liquid water via anion threshold photodetachment and above threshold solvent ionization
    • Vilchiz V.H., Kloepfer J.A., Germaine A.C., Lenchenkov V.A., Bradforth S.E. Map for the relaxation dynamics of hot photoelectrons injected into liquid water via anion threshold photodetachment and above threshold solvent ionization. J. Phys. Chem., A. 105:2001;1711-1723
    • (2001) J. Phys. Chem., a , vol.105 , pp. 1711-1723
    • Vilchiz, V.H.1    Kloepfer, J.A.2    Germaine, A.C.3    Lenchenkov, V.A.4    Bradforth, S.E.5
  • 88
    • 0031200572 scopus 로고    scopus 로고
    • Parameter precision in global analysis of time resolved spectra
    • van Stokkum I.H.M. Parameter precision in global analysis of time resolved spectra. IEEE Trans. Instrum. Meas. 46:1997;764-768
    • (1997) IEEE Trans. Instrum. Meas. , vol.46 , pp. 764-768
    • Van Stokkum, I.H.M.1
  • 91
    • 0037305871 scopus 로고    scopus 로고
    • Deuterium isotope effects in the photocycle transitions of the photoactive yellow protein
    • Hendriks J., van Stokkum I.H.M., Hellingwerf K.J. Deuterium isotope effects in the photocycle transitions of the photoactive yellow protein. Biophys. J. 84:2003;1180-1191
    • (2003) Biophys. J. , vol.84 , pp. 1180-1191
    • Hendriks, J.1    Van Stokkum, I.H.M.2    Hellingwerf, K.J.3
  • 94
    • 0001170301 scopus 로고    scopus 로고
    • Reorientation of the retinylidene chromophore in the K, L, and M intermediates of bacteriorhodopsin from time-resolved linear dichroism: Resolving kinetically and spectrally overlapping intermediates of chromoproteins
    • Borucki B., Otto H., Heyn M.P. Reorientation of the retinylidene chromophore in the K, L, and M intermediates of bacteriorhodopsin from time-resolved linear dichroism: resolving kinetically and spectrally overlapping intermediates of chromoproteins. J. Phys. Chem., B. 103:1999;6371-6383
    • (1999) J. Phys. Chem., B , vol.103 , pp. 6371-6383
    • Borucki, B.1    Otto, H.2    Heyn, M.P.3
  • 95
    • 0034734261 scopus 로고    scopus 로고
    • Chromophore reorientation during the photocycle of bacteriorhodopsin: Experimental methods and functional significance
    • Heyn M.P., Borucki B., Otto H. Chromophore reorientation during the photocycle of bacteriorhodopsin: experimental methods and functional significance. Biochim. Biophys. Acta. 1460:2000;60-74
    • (2000) Biochim. Biophys. Acta , vol.1460 , pp. 60-74
    • Heyn, M.P.1    Borucki, B.2    Otto, H.3
  • 97
    • 0029757121 scopus 로고    scopus 로고
    • Ultra-fast excited state dynamics in green fluorescent protein: Multiple states and proton transfer
    • Chattoraj M., King B.A., Bublitz G.U., Boxer S.G. Ultra-fast excited state dynamics in green fluorescent protein: Multiple states and proton transfer. Proc. Nat. Acad. Sci. U. S. A. 93:1996;8362-8367
    • (1996) Proc. Nat. Acad. Sci. U. S. A. , vol.93 , pp. 8362-8367
    • Chattoraj, M.1    King, B.A.2    Bublitz, G.U.3    Boxer, S.G.4
  • 99
    • 0000803444 scopus 로고
    • The differentiation of pseudo-inverses and nonlinear least squares problems whose variables separate
    • Golub G.H., Pereyra V. The differentiation of pseudo-inverses and nonlinear least squares problems whose variables separate. SIAM J. Numer. Anal. 10:1973;413-432
    • (1973) SIAM J. Numer. Anal. , vol.10 , pp. 413-432
    • Golub, G.H.1    Pereyra, V.2
  • 100
    • 0016450838 scopus 로고
    • A variable projection method for solving separable nonlinear least squares problems
    • Kaufman L. A variable projection method for solving separable nonlinear least squares problems. BIT. 15:1975;49-57
    • (1975) BIT , vol.15 , pp. 49-57
    • Kaufman, L.1
  • 102
    • 3242676010 scopus 로고
    • A semi-linear optimization model for resolving fast processes
    • Solar S., Solar W., Getoff N. A semi-linear optimization model for resolving fast processes. J. Chem. Soc., Faraday Trans. 2, 79:1983;123-135
    • (1983) J. Chem. Soc., Faraday Trans. , vol.279 , pp. 123-135
    • Solar, S.1    Solar, W.2    Getoff, N.3
  • 103
    • 0028672974 scopus 로고
    • Determining confidence intervals for parameters derived from analysis of equilibrium analytical ultracentrifugation data
    • Brooks I., Watts D.G., Soneson K.K., Hensley P. Determining confidence intervals for parameters derived from analysis of equilibrium analytical ultracentrifugation data. Methods Enzymol. 240:1994;459-478
    • (1994) Methods Enzymol. , vol.240 , pp. 459-478
    • Brooks, I.1    Watts, D.G.2    Soneson, K.K.3    Hensley, P.4
  • 105
    • 85111791877 scopus 로고    scopus 로고
    • A Problem Solving Environment for interactive modelling of multiway data
    • accepted for publication.
    • I.H.M. van Stokkum, H.E. Bal, A Problem Solving Environment for interactive modelling of multiway data, Concurrency Computat: Pract. Exper., accepted for publication.
    • Concurrency Computat: Pract. Exper.
    • Van Stokkum, I.H.M.1    Bal, H.E.2
  • 106
    • 0031808072 scopus 로고    scopus 로고
    • New photocycle intermediates in the photoactive yellow protein from Ectothiorhodospira halophila: Picosecond transient absorption spectroscopy
    • Ujj L., Devanathan S., Meyer T.E., Cusanovich M.A., Tollin G., Atkinson G.H. New photocycle intermediates in the photoactive yellow protein from Ectothiorhodospira halophila: picosecond transient absorption spectroscopy. Biophys. J. 75:1998;406-412
    • (1998) Biophys. J. , vol.75 , pp. 406-412
    • Ujj, L.1    Devanathan, S.2    Meyer, T.E.3    Cusanovich, M.A.4    Tollin, G.5    Atkinson, G.H.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.