City Research Online

Fluorescent labelling of proteins - Volume 2

Chappell, D. C. (1991). Fluorescent labelling of proteins - Volume 2. (Unpublished Doctoral thesis, City, University of London)


Investigations were also undertaken in order to gain a fuller understanding of the process of fluorescence quenching via resonance energy transfer. In order to achieve this, tetramethylrhodamine dimers and fluorescein dimers were produced in aqueous solution, whereby excited state energy from the fluorescein chromophore is donated to the tetramethylrhodamine chromophore. Also, a series of proteins were fluorescently modified via lysine residues with these reagents, and the resultant absorption and fluorescence spectra were examined.

A natural fluorescence quencher of both intrinsic and extrinsic fluorescent species is the haem moiety of the haemoproteins. Horseradish peroxidase isoenzyme C, was investigated with regard to its efficiency in this respect. Partial fluorescent modification of the enzyme was achieved, utilising amine-reactive fluorescein and organometallic chromophores, as the extrinsic fluorescent species. The distance between the haem centre and the respective fluorophore was calculated, and the position of the reactive lysine residue was suggested.

Publication Type: Thesis (Doctoral)
Subjects: Q Science > QD Chemistry
Departments: Doctoral Theses
School of Science & Technology
School of Science & Technology > School of Science & Technology Doctoral Theses
[thumbnail of Chappell thesis 1991 Vol 2 PDF-A.pdf]
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