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Biological chromophores

The main drawback to the INDO-1 system is autofluorescence from the sample, arising from competitive excitation of biological chromophores. If the ligand has another fault, it is that it binds so strongly to calcium that it might buffer the metal ion concentration under certain... [Pg.915]

Biological chromophores have characteristic UV/visible absorbance and fluorescence spectra that can give general information about molecular environments. [Pg.66]

Surface Enhanced Raman Scattering of Biomolecules Table 5. Resonance Raman spectroscopy of biological chromophores (SERRS studies are underlined)... [Pg.41]

Gostkowski, M. L., McDoniel, J. B., Wei, J., Curey, T. E., and Shear, J. B., Characterizing spectrally diverse biological chromophores using capillary electrophoresis with multiphoton-excited fluorescence, J. Am. Ghem. Soc., 120, 18, 1998. [Pg.329]

Martinez TJ (2006) Insights for light-driven molecular devices from ab initio multiple spawning excited-state dynamics of organic and biological chromophores. Acc Chem Res 39 119... [Pg.334]

Biological systems (e.g., proteins, cells) excited at wavelengths below 500 nm produce considerable autofluorescence that arises mainly from flavins, flavoproteins, NADH, etc. Labels that can be excited at wavelengths above 500 nm are much less susceptible to optical interference from biological chromophores in the test sample. [Pg.1385]

Elucidation of Protein Structure UV absorption has been used to study the intra-and intermolecular interactions of biological chromophores in different environments. These interactions are often manifested in the shapes of macromolecules. For example, poly-L-lysine hydrochloride exists in three dfferent forms in aqueous solution, depending on the pH and temperature of the solution random cod, pH 6.0, 25°C helix, pH 10.8, 25 C and p-form, pH 10.8,52°C. The UV absorption spectra of poly-L-lysine hydrochloride for these three forms are shown in Figure 17.5. [Pg.407]

Marques MAL, L6pez X, Varsano D, Castro A, Rubio A (2003) Time-dependent density-functional approach for biological chromophores the ease of the green fluorescent protein. Phys Rev Lett 90(25) 258101-258104... [Pg.222]


See other pages where Biological chromophores is mentioned: [Pg.413]    [Pg.915]    [Pg.135]    [Pg.329]    [Pg.86]    [Pg.227]    [Pg.466]    [Pg.486]    [Pg.1497]    [Pg.96]    [Pg.33]    [Pg.339]    [Pg.191]    [Pg.191]    [Pg.611]    [Pg.40]    [Pg.41]    [Pg.325]    [Pg.332]    [Pg.333]    [Pg.1367]    [Pg.56]    [Pg.457]   
See also in sourсe #XX -- [ Pg.466 ]




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