A modified clear-native polyacrylamide gel electrophoresis technique to investigate the oligomeric state of MBP-5-HT3A-intracellular domain chimeras.

Abstract:

:The main principles of higher-order protein oligomerization are elucidated by many structural and biophysical studies. An astonishing number of proteins self-associate to form dimers or higher-order quaternary structures which further interact with other biomolecules to elicit complex cellular responses. In this study, we describe a simple and convenient approach to determine the oligomeric state of purified protein complexes that combines implementation of a novel form of clear-native gel electrophoresis and size exclusion chromatography in line with multi-angle light scattering. Here, we demonstrate the accuracy of this ensemble approach by characterizing the previously established pentameric state of the intracellular domain of serotonin type 3A (5-HT3A) receptors.

journal_name

Protein Expr Purif

authors

Pandhare A,Stuebler AG,Pirayesh E,Jansen M

doi

10.1016/j.pep.2018.08.010

subject

Has Abstract

pub_date

2019-01-01 00:00:00

pages

45-52

eissn

1046-5928

issn

1096-0279

pii

S1046-5928(18)30370-X

journal_volume

153

pub_type

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