Optimal fluorescent protein tags for quantifying protein oligomerization in living cells.

ABSTRACT: Fluorescence fluctuation spectroscopy has become a popular toolbox for non-disruptive analysis of molecular interactions in living cells. The quantification of protein oligomerization in the native cellular environment is highly relevant for a detailed understanding of complex biological processes. An important parameter in this context is the molecular brightness, which serves as a direct measure of oligomerization and can be easily extracted from temporal or spatial fluorescence fluctuations. However, fluorescent proteins (FPs) typically used in such studies suffer from complex photophysical transitions and limited maturation, inducing non-fluorescent states. Here, we show how these processes strongly affect molecular brightness measurements. We perform a systematic characterization of n

SUBMITTER: Dunsing V 

PROVIDER: S-EPMC6045628 | biostudies-literature | 2018 Jul

REPOSITORIES: biostudies-literature