The electronic spectrum of the fluoroborane free radical. II. Analysis of laser-induced fluorescence and single vibronic level emission spectra

2009 ◽  
Vol 130 (16) ◽  
pp. 164310 ◽  
Author(s):  
Fumie X. Sunahori ◽  
Dennis J. Clouthier
2004 ◽  
Vol 121 (3) ◽  
pp. 1405-1411 ◽  
Author(s):  
Brandon S. Tackett ◽  
Dennis J. Clouthier ◽  
Allan G. Adam ◽  
Scott A. Shepard

2016 ◽  
Vol 144 (18) ◽  
pp. 184303 ◽  
Author(s):  
Daniel K. W. Mok ◽  
Edmond P. F. Lee ◽  
John M. Dyke

2004 ◽  
Vol 120 (3) ◽  
pp. 1292-1305 ◽  
Author(s):  
Daniel K. W. Mok ◽  
Edmond P. F. Lee ◽  
Foo-tim Chau ◽  
John M. Dyke

2006 ◽  
Vol 2006 ◽  
pp. 1-5 ◽  
Author(s):  
Austin Nevin ◽  
Demetrios Anglos

Laser-induced fluorescence (LIF) spectroscopy can provide nondestructive, qualitative analysis of protein-based binding media found in artworks. Fluorescence emissions from proteins in egg yolk and egg white are due to autofluorescent aromatic amino acids as well as other native and age-related fluorophores, but the potential of fluorescence spectroscopy for the differentiation between binding media is dependent on the choice of a suitable excitation wavelength and limited by problems in interpretation. However, a better understanding of emission spectra associated with LIF can be achieved following comparisons with total emission fluorescence spectra where a series of consecutive emission spectra are recorded over a specific range. Results using nanosecond UV laser sources for LIF of egg-based binding media are presented which are rationalised following comparisons with total emission spectra. Specifically, fluorescence is assigned to tryptophan and oxidation products of amino acids; in the case of egg yolk, fatty-acid polymerisation and age-related degradation products account for the formation of fluorophores.


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