Share Email Print

Proceedings Paper

Aggregation strongly influences the pH-profile of the fluorescence of yellow fluorescent protein zFP538
Author(s): Nadya N. Zubova; Natalia V. Rudenko; Alexander P. Savitsky
Format Member Price Non-Member Price
PDF $17.00 $21.00

Paper Abstract

Fluorescence of the yellow fluorescent protein zFP538 strongly depends on concentration and starting pH form which pH profile is recorded. pH transitions typical for chromopeptides isolated from zFP538 can be observed for whole protein in diluted solutions. The quenching fluorescence of zFP538 is irreversible upon acidification or alkalization of the low concentrated soultions. In concentrated solutions, according to the data of dynamic light scattering, the protein zFP538 is strongly aggretaed (or oligomerized) and become more stable against acid denaturation. Spectral changes on pH are almost reversible both for fluorescence and absorbance. Two major chromopeptides obtained from zFP538 have different spectral properties and no similarity to the spectral properties of the chromopeptide obtained from GFP.

Paper Details

Date Published: 12 September 2003
PDF: 12 pages
Proc. SPIE 4967, Genetically Engineered and Optical Probes for Biomedical Applications, (12 September 2003); doi: 10.1117/12.485818
Show Author Affiliations
Nadya N. Zubova, M.V. Lomonosov Moscow State Univ. (Russia)
Natalia V. Rudenko, Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, RAS (Russia)
Alexander P. Savitsky, A.N. Bach Institute of Biochemistry (Russia)

Published in SPIE Proceedings Vol. 4967:
Genetically Engineered and Optical Probes for Biomedical Applications
Darryl J. Bornhop; Alexander P. Savitsky; Ramesh Raghavachari; Samuel I. Achilefu, Editor(s)

© SPIE. Terms of Use
Back to Top
Sign in to read the full article
Create a free SPIE account to get access to
premium articles and original research
Forgot your username?