S1 and S2 excited States of gas-phase Schiff-base retinal chromophores.
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[1] S. Nielsen,et al. Gas-phase absorption properties of a green fluorescent protein-mutant chromophore: The W7 clone , 2003 .
[2] Shigeyoshi Yamamoto,et al. Ab initio MO study on the potential energy surfaces of low-lying excited states of protonated Schiff base retinal , 1998 .
[3] F. Bernardi,et al. The retinal chromophore/chloride ion pair: structure of the photoisomerization path and interplay of charge transfer and covalent states. , 2005, Proceedings of the National Academy of Sciences of the United States of America.
[4] L. H. Andersen,et al. Physics with electrostatic rings and traps , 2004 .
[5] D. Oesterhelt,et al. Rhodopsin-like protein from the purple membrane of Halobacterium halobium. , 1971, Nature: New biology.
[6] R. Birge,et al. Two‐photon double resonance spectroscopy of bacteriorhodopsin. Assignment of the electronic and dipolar properties of the low‐lying 1A*−g‐like and 1B*+u‐like π, π* states , 1990 .
[7] Steen Brøndsted Nielsen,et al. Chromophores of the green fluorescent protein studied in the gas phase , 2002 .
[8] Stefan Haacke,et al. Absorption of schiff-base retinal chromophores in vacuo. , 2005, Journal of the American Chemical Society.
[9] P. Anfinrud,et al. The photoisomerization of retinal in bacteriorhodospin: experimental evidence for a three-state model. , 1996, Proceedings of the National Academy of Sciences of the United States of America.
[10] G. E. Leroi,et al. Two-photon spectroscopy of all-trans-retinal. Nature of the low-lying singlet states , 1982 .
[11] D. Oesterhelt,et al. Closing in on bacteriorhodopsin: progress in understanding the molecule. , 1999, Annual review of biophysics and biomolecular structure.
[12] P. Tonge,et al. Gas-phase absorption properties of DsRed model chromophores , 2003 .
[13] T. Jørgensen,et al. The combination of an electrospray ion source and an electrostatic storage ring for lifetime and spectroscopy experiments on biomolecules , 2002 .
[14] J U Andersen,et al. Absorption spectrum of the green fluorescent protein chromophore anion in vacuo. , 2001, Physical review letters.
[15] Marco Garavelli,et al. Structure, spectroscopy, and spectral tuning of the gas-phase retinal chromophore: the beta-ionone "handle" and alkyl group effect. , 2005, The journal of physical chemistry. A.
[16] M Olivucci,et al. Computational evidence in favor of a two-state, two-mode model of the retinal chromophore photoisomerization. , 2000, Proceedings of the National Academy of Sciences of the United States of America.
[17] G. Wald. The molecular basis of visual excitation. , 1968, Nature.
[18] P. Tonge,et al. Vibrationally resolved photoabsorption spectroscopy of red fluorescent protein chromophore anions. , 2003, Physical review letters.
[19] S. Møller. ELISA, and electrostatic storage ring for atomic physics , 1997 .
[20] L. P. Murray,et al. Two-photon, carbon-13 and two-dimensional proton NMR spectroscopic studies of retinyl Schiff bases, protonated Schiff bases and Schiff base salts: evidence for a protonation induced .pi..pi.* excited state level ordering reversal , 1987 .
[21] Hideki Kandori,et al. Femtosecond fluorescence study of the rhodopsin chromophore in solution , 1995 .
[22] Riccardo Basosi,et al. Properties of the emitting state of the green fluorescent protein resolved at the CASPT2//CASSCF/CHARMM level. , 2005, Journal of the American Chemical Society.
[23] C. H. Brito Cruz,et al. Direct observation of the femtosecond excited-state cis-trans isomerization in bacteriorhodopsin. , 1988, Science.
[24] L. P. Murray,et al. Two-photon spectroscopy of locked-11-cis-rhodopsin: evidence for a protonated Schiff base in a neutral protein binding site. , 1985, Proceedings of the National Academy of Sciences of the United States of America.
[25] T. Jørgensen,et al. Experimental studies of the photophysics of gas-phase fluorescent protein chromophores , 2004 .
[26] K. Hansen,et al. On the concept of temperature for a small isolated system , 2001 .