[1]
|
Demchenko, A.P. (1986) Ultrasiolet spectroscopy of proteins. Springer-Verlag, New York.
|
[2]
|
Eftink, M.R. (1991) Fluorescence techniques for studying protein structure. Methods of Biochemical Analysis, 35, 127-205. doi:10.1002/9780470110560.ch3
|
[3]
|
Weber, G. (1960) Fluorescence-polarization spectrum and electronic energy transfer in tyrosine, tryptophan and related compounds. Biochemical Journal, 75, 335-345.
|
[4]
|
Konev, S.V. (1967) Fluorescence and phosphorescence of proteins and nucleic acids. Plenum, New York.
|
[5]
|
Beechem, J.M. and Brand, L. (1985) Time-resolved fluorescence of proteins. Annual Review of Biochemistry, 54, 43-71. doi:10.1146/annurev.bi.54.070185.000355
|
[6]
|
Muí?o, P.L. and Callis, P.R. (1994) Hybrid simulations of salvation effects on electronic spectra: Indoles in water. Journal of Chemical Physics, 100, 4093-4109.
|
[7]
|
Callis, P.R. (1997) 1La and 1Lb transitions of tryptophan: Applications of theory and experimental observations to fluorescence of proteins. Methods in Enzymology, 278, 113-150. doi:10.1016/S0076-6879(97)78009-1
|
[8]
|
Chen Y. and Barkley, M.D. (1998) Toward understanding tryptophan fluorescence in proteins. Biochemistry, 37, 9976-9982. doi:10.1021/bi980274n
|
[9]
|
Vivian, J.T. and Callis, P.R. (2001) Mechanisms of tryptophan fluorescence shifts in proteins. Biophysical Journal, 80, 2093-2109. doi:10.1016/S0006-3495(01)76183-8
|
[10]
|
Toptygin, D., Savtchenko, R.S., Meadow, N.D. and Brand, L. (2001) Homogeneous spectrally- and time-resolved fluorescence emission from single-tryptophan mutants of IIAGlc. Journal of Physical Chemistry B, 105, 2043-2055.
doi:10.1021/jp003405e
|
[11]
|
Xu, J., Chen, J., Toptygin, D., Tcherkasskaya, O., Callis, P.R., King, J., Brand, L. and Knutson, J.R. (2009) Femtosecond fluorescence spectra of tryptophan in human γ-crystallin mutants: Site-dependent ultrafast quenching. Journal of the American Chemical Society, 131, 16751- 16757. doi:10.1021/ja904857t
|
[12]
|
Cowgill, R.W. (1970) Fluorescence and protein structure. XVII. On the mechanism of peptide quenching. Biochimica et Biophysica Acta, 200, 18-25.
|
[13]
|
Feitelson, J. (1970) Environmental effects on the fluorescence of tryptophan and other indole derivatives. Israel Journal of Chemistry, 8, 241-252.
|
[14]
|
Petrich, J.W., Chang, M.C., McDonald, D.D. and Fleming, G.R. (1983) On the origin of nonexponential fluorescence decay in tryptophan and its derivatives. Journal of the American Chemical Society, 105, 3824-3832.
doi:10.1021/ja00350a014
|
[15]
|
Chen, Y., Liu, B., Yu, H.T., Barkley, M.D. (1996) The peptide bond quenches indole fluorescence. Journal of the American Chemical Society, 118, 9271-9278.
doi:10.1021/ja961307u
|
[16]
|
Sillen, A., Hennecke, J., Roethlisberger, D., Glockshuber, R. and Engelborghs, Y. (1999) Fluorescence quenching in the DsbA protein from E. coli: Complete picture of the excited-state energy pathway and evidence for the reshuffling dynamics of the microstates of tryptophan. Proteins: Structure, Function, and Genetics. 37, 253-263.
doi:10.1002/(SICI)1097-0134(19991101)37:2<253::AID-PROT10>3.0.CO;2-J
|
[17]
|
Vivian, J.T. and Callis, P.R. (2002) Understanding the variable fluorescence quantum yield of tryptophan in proteins using QM-MM simulations. Quenching by charge transfer to the peptide backbone. Chemical Physics Letters, 369, 409-414.
|
[18]
|
Callis, P.R., Liu, T. (2004) Quantitative prediction of fluorescence quantum yields for tryptophan in proteins. Journal of Physical Chemistry B, 108, 4248-4259.
doi:10.1021/jp0310551
|
[19]
|
Callis, P.R., Petrenko, A., Muí?o, P.L., Tusell, J.R. (2007) Ab Initio prediction of tryptophan fluorescence quenching by protein electric field-enabled electron transfer. Journal of Physical Chemistry B, 111, 10335-10339.
doi:10.1021/jp0744883
|
[20]
|
Muí?o, P.L. and Callis, P.R. (2009) Solvent effects on the fluorescence quenching of tryptophan by amides via electron transfer. Experimental and computational studies. Journal of Physical Chemistry B, 113, 2572-2577.
doi:10.1021/jp711513b
|
[21]
|
Pan, C.P., Muí?o, P.L., Barkley, M.D. and Callis, P.R. (2011) Correlation of tryptophan fluorescence spectral shifts and lifetimes arising directly from heterogeneous environment. Journal of Physical Chemistry B, 115, 3245-3253. doi:10.1021/jp111925w
|
[22]
|
Chen, R., Knutson, J.R., Ziffer, H. and Porter, D. (1991) Fluorescence of tryptophan dipeptides: Correlations with the rotamer model. Biochemistry, 30, 5184-5195. doi:10.1021/bi00235a011
|
[23]
|
Xu, J. and Knutson, J.R. (2009) Quasi-static self- quenching of Trp-X and X-Trp dipeptides in water: Ultrafast fluorescence decay. Journal of Physical Chemistry B, 113, 12084-12089. doi:10.1021/jp903078x
|
[24]
|
Yu, H.T., Colucci, W.J., McLaughlin, M.L. and Barkley, M.D. (1992) Fluorescence quenching of indoles by excited state proton transfer. Journal of the American Chemical Society, 114, 8449-8454.
doi:10.1021/ja00048a015
|
[25]
|
Eftink, M.R., Jia, Y., Hu, D. and Ghiron, J.A. (1995) Fluorescence studies with tryptophan analogs: Excited state interactions involving the side chain amino group. Journal of Physical Chemistry, 99, 5713-5723.
doi:10.1021/j100015a064
|
[26]
|
Dawson, R.M.C., Elliot, D.C., Elliot, W.H. and Jones, K. M. (1986) Data for biochemical research. Clarendon Press, Oxford.
|
[27]
|
Blancafort, L., González, D., Olivucci, M., Robb, M.A. (2002) Quenching of tryptophan 1(π,π*) fluorescence induced by intramolecular hydrogen abstraction via an aborted decarboxylation mechanism. Journal of the American Chemical Society, 124, 6398-6406.
doi:10.1021/ja016915a
|
[28]
|
Sobolewski, A.L. and Domcke, W. (1999) Ab initio investigations on the photophysics of indole. Chemical Physics Letters. 315, 293-298.
doi:10.1016/S0009-2614(99)01249-X
|