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Proceedings Paper

Definition of the energy map and its applications to the study of chromophores in proteins
Author(s): Andras D. Kaposi; V. Logovinsky; Jane M. Vanderkooi
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Paper Abstract

The porphyrin in metal-free cytochrome c molecules was investigated using fluorescence line narrowing spectroscopy. An energy map is defined to illustrate the environmental effects on the vibronic structure of a chromophore. In the approximation of pure electronic distortion, the population distribution in the energy scale can be characterized by a function. An intuitive definition of this distribution function is determined for the porphyrin in cytochrome c, and the validity of this approximation is experimentally verified. In addition, numerous excited state vibrational levels suggest a method to quantify the relative absorption probabilities for (0,0)yields(1,k) transitions.

Paper Details

Date Published: 1 April 1992
PDF: 8 pages
Proc. SPIE 1640, Time-Resolved Laser Spectroscopy in Biochemistry III, (1 April 1992); doi: 10.1117/12.58275
Show Author Affiliations
Andras D. Kaposi, Univ. of Pennsylvania (United States)
V. Logovinsky, Univ. of Pennsylvania (United States)
Jane M. Vanderkooi, Univ. of Pennsylvania (United States)

Published in SPIE Proceedings Vol. 1640:
Time-Resolved Laser Spectroscopy in Biochemistry III
Joseph R. Lakowicz, Editor(s)

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