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Chromophores green fluorescent proteins

Martin ME, Negri F, Olivucci M (2004) Origin, nature, and fate of the fluorescent state of the green fluorescent protein chromophore at the CASPT2//CASSCF resolution. J Am Chem Soc 126 5452... [Pg.328]

Mandal D, Tahara T, Meech SR (2004) Excited-state dynamics in the green fluorescence protein chromophore. J Phys Chem B 108 1102-1108... [Pg.264]

Barondeau DP, Putnam CD, Kassmann CJ, Tainer JA, Getzoff ED (2003) Mechanism and energetics of green fluorescent protein chromophore synthesis revealed by trapped intermediate structures. Proc Natl Acad Sci USA 100 12111-12116... [Pg.375]

Bell AF, He X, Wachter RM, Tonge PJ (2000) Probing the ground state structure of the green fluorescent protein chromophore using Raman spectroscopy. Biochemistry 39 4423 1431... [Pg.375]

He X, Bell AF, Tonge PJ (2002) Isotopic labeling and normal-mode analysis of a model green fluorescent protein chromophore. J Phys Chem B 106 6056-6066... [Pg.375]

Yang JS, Huang GJ, Liu YH, Peng SM (2008) Photoisomerization of the green fluorescence protein chromophore and the meta- and para-amino analogues. Chem Commun 1344-1346... [Pg.376]

Flelms V, Winstead C, Langhoff PW (2000) Low-lying electronic excitations of the green fluorescent protein chromophore. Theochem-J Mol Struct 506 179-189... [Pg.377]

Webber NM, Litvinenko KL, Meech SR (2001) Radiationless relaxation in a synthetic analogue of the green fluorescent protein chromophore. J Phys Chem B 105 8036-8039... [Pg.377]

Usman A, Mohammed OP, Nibbering ET, Dong J, Solntsev KM, Tolbert LM (2005) Excited-state structure determination of the green fluorescent protein chromophore. J Am Chem Soc 127 11214-11215... [Pg.377]

Altoe P, Bemardi F, Garavelli M, Orlandi G, Negri F (2005) Solvent effects on the vibrational activity and photodynamics of the green fluorescent protein chromophore a quantum-chemical study. J Am Chem Soc 127 3952-3963... [Pg.377]

Ultrafast excited state dynamics in the green fluorescent protein chromophore... [Pg.425]

Fig. 5.4 The r (N1-C1-C2-C3) and q> (Cl-C2-C3-C4) dihedral angles of the green fluorescent protein chromophore. In the protein R, is Gly67 and R2 is Ser65, and in HBDI, an often used model compound, = R2 = CH3. In r one-bond flips (r-OBF) the dihedral rotation occurs around the r torsional angle, in a (p-OBF it is around the (p dihedral angle, in a hula twist (HT) the (p and r dihedral angles concertedly rotate. Fig. 5.4 The r (N1-C1-C2-C3) and q> (Cl-C2-C3-C4) dihedral angles of the green fluorescent protein chromophore. In the protein R, is Gly67 and R2 is Ser65, and in HBDI, an often used model compound, = R2 = CH3. In r one-bond flips (r-OBF) the dihedral rotation occurs around the r torsional angle, in a (p-OBF it is around the (p dihedral angle, in a hula twist (HT) the (p and r dihedral angles concertedly rotate.
Fig. 5.5 Models of the green fluorescent protein chromophore in the neutral, anionic, and zwitterionic forms used in the quantum chemical calculations, shown in those resonance structures that best represent the calculated bond orders. Rotation by 180° around (p leaves the structure unchanged. The configurations displayed represent r = 0° and are referred to as cis configurations. The upper panels show energy profiles for rotation around the dihedral angles r and (p and for... Fig. 5.5 Models of the green fluorescent protein chromophore in the neutral, anionic, and zwitterionic forms used in the quantum chemical calculations, shown in those resonance structures that best represent the calculated bond orders. Rotation by 180° around (p leaves the structure unchanged. The configurations displayed represent r = 0° and are referred to as cis configurations. The upper panels show energy profiles for rotation around the dihedral angles r and (p and for...
Fig. 12.5. Ball and stick representation of the green fluorescent protein chromophore (left side) as an example of molecule which can waste the photon energy and of the visual pigment rhodopsin chromophore (right side) which can efficiently convert the light energy into molecular motion (adapted from Ref. [8]). Fig. 12.5. Ball and stick representation of the green fluorescent protein chromophore (left side) as an example of molecule which can waste the photon energy and of the visual pigment rhodopsin chromophore (right side) which can efficiently convert the light energy into molecular motion (adapted from Ref. [8]).
Accurate calculations for excitations with DMC are possible for systems as large as free-base porphyrin and models of the green fluorescent protein chromophore. Drummond et al. investigated the electron emission from diamondoids with DMC. Using DFT orbitals in DMC, they calculated the excitation energy for the HOMO-LUMO transition (optical gap), the electron affinity, and the ionization potential for carbon clusters with diamond structure up to CgvHvs. ... [Pg.254]

Mandal, D., Tahara, T., Meech, S.R. Excited-state dynamics in the green fluorescent protein chromophore. J. Phys. (Them. B 108, 1102-1108 (2004)... [Pg.289]

E. Epifanovsky, 1. Polyakov, B. Grigorenko, A. Nemukhin, and A. 1. Krylov,/. Chem. Theory Comput., 5,1895—1906 (2009). Quantum Chemical Benchmark Studies of the Electronic Properties of the Green Fluorescent Protein Chromophore. 1. Electronically Excited and Ionized States of the Anionic Chromophore in the Gas Phase. [Pg.516]

Vision involves cis-trans photoisomerization of a chromophore and many studies have been done using different models/ For example, a CASSCF/AMBER procedure has been used to study the nonadiabatic dynamics of retinal in rhodopsin proteins/ In another study, a simple model of a photosynthetic center was examined by Worth and Cederbaum. They proposed that the presence of conical intersections facilitated the long-range intermolecular photo-initiated electron transfer between the protein s porphyrin and a nearby quinone. Semiempirical methods and QM/MM methods have been developed by Martinez and coworkers " to study the cis-trans isomerization dynamics of the Green Fluorescent Protein chromophore in solution, which occurs through conical intersections.The chromophore in this protein consists of two rings connected with a double bond and has been studied in vacuo as well. ... [Pg.107]

Nature, and Fate of the Fluorescent State of the Green Fluorescent Protein Chromophore at the CASPT2//CASSCF Resolution. [Pg.122]

See other pages where Chromophores green fluorescent proteins is mentioned: [Pg.544]    [Pg.1145]    [Pg.2716]   
See also in sourсe #XX -- [ Pg.258 , Pg.515 ]



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Fluorescence chromophores

Fluorescence green fluorescent protein

Fluorescence proteins

Fluorescent chromophore

Fluorescent proteins

Green chromophore

Green fluorescence protein

Green fluorescent protein

Green fluorescent protein proteins

Protein chromophores

Protein fluorescer

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