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Title: Temperature-pressure stability of green fluorescent protein: A Fourier transform infrared spectroscopy study
Authors: Scheyhing, CH *
Meersman, Filip * ×
Ehrmann, MA
Heremans, Karel
Vogel, RF #
Issue Date: Jan-2002
Publisher: John wiley & sons inc
Series Title: Biopolymers vol:65 issue:4 pages:244-253
Abstract: Green fluorescent protein (GFP) is widely used as a marker in molecular and cell biology. For its use in high-pressure microbiology experiments, its fluorescence under pressure was recently investigated. Changes in fluorescence with pressure were found. To find out whether these are related to structural changes, we investigated the pressure stability of wild-type GFP (wtGFP) and three of its red shift mutants (AFP, GFP(mut1) and GFP(mut2)) using Fourier transform infrared spectroscopy. For the wt GFP, GFP(mut1), and GFP(mut2) we found that up to 13-14 kbar the secondary structure remains intact, whereas AFP starts unfolding around 10 kbar. The 3-D structure is held responsible for this high-pressure stability. Previously observed changes in fluorescence at low pressure are rationalized in terms of the pressure-induced elastic effect. Above 6 kbar, loss of fluorescence is due to aggregation. Revisiting the temperature stability of GFP, we found that an intermediate state is populated along the unfolding pathway of wtGFP. At higher temperatures, the unfolding resulted in the formation of aggregates of wtGFP and its mutants. (C) 2002 Wiley Periodicals, Inc.
URI: 
ISSN: 0006-3525
Publication status: published
KU Leuven publication type: IT
Appears in Collections:Molecular Imaging and Photonics
Biochemistry, Molecular and Structural Biology Section
* (joint) first author
× corresponding author
# (joint) last author

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