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Use of carbonate extraction in analyzing moderately hydrophobic transmembrane proteins in the mitochondrial inner membrane
Author(s) -
Kim Hayoung,
Botelho Salomé Calado,
Park Kwangjin,
Kim Hyun
Publication year - 2015
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1002/pro.2817
Subject(s) - inner mitochondrial membrane , translocase of the inner membrane , integral membrane protein , inner membrane , transmembrane protein , extraction (chemistry) , carbonate , membrane , biophysics , chemistry , transmembrane domain , membrane protein , sodium carbonate , mitochondrion , biochemistry , chromatography , biology , mitochondrial membrane transport protein , sodium , organic chemistry , receptor
Abstract Resistance to sodium carbonate extraction is regarded as a canonical way to distinguish integral membrane proteins (MPs) from other membrane‐associated proteins. However, it has been observed that carbonate extraction releases some mitochondrial integral MPs. Here, by analyzing both artificially designed and native mitochondrial inner MPs containing transmembrane domains (TMDs) of different hydrophobicities, we show that carbonate treatment can release moderately hydrophobic TMDs from the mitochondrial inner membrane. These results suggest that resistance and sensitivity to carbonate extraction may be interpreted with caution when analyzing the nature of mitochondrial inner MPs.