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Can the fluorescence of green fluorescent protein chromophore be related directly to the nativity of protein structure?

Abstract：

:In studies of green fluorescence protein (GFP) or other proteins with the use of GFP as a marker, the fluorescence of GFP is for the most part related directly to the nativity of its structure. Naturally, such a relation does exist since the chromophore of this protein is formed autocatalytically only just after GFP acquires its native structure. However, the fluorescence method may not yield reliable information on protein structure when studying renaturation and denaturation of this protein (with the formed chromophore). Using proteolysis, denaturant gradient gel electrophoresis and circular dichroism, we demonstrate herein that at major disturbances of the native structure of protein GFP-cycle3 the intensity of fluorescence of its chromophore can change insignificantly. In other words, the chromophore fluorescence does not reliably mirror alterations in protein structure. Since the main conclusions of this study are especially qualitative, it can be suggested that during renaturation/denaturation of wild-type GFP and its "multicolored" mutants their fluorescence is also not always associated with the changes in the structure of these proteins.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Melnik BS,Povarnitsyna TV,Melnik TN

doi

10.1016/j.bbrc.2009.10.109

subject

Has Abstract

pub_date

2009-12-25 00:00:00

pages

1167-70

issue

4

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(09)02100-7

journal_volume

390

pub_type

杂志文章

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