Use of carbonate extraction in analyzing moderately hydrophobic transmembrane proteins in the mitochondrial inner membrane
| Autor: | Hayoung Kim, Hyun Kim, Kwangjin Park, Salomé Calado Botelho |
|---|---|
| Rok vydání: | 2015 |
| Předmět: |
congenital
hereditary and neonatal diseases and abnormalities Binding Sites Methods and Applications Carbonates Membrane Proteins nutritional and metabolic diseases Mitochondrion Biology Mitochondrial carrier Biochemistry Transmembrane protein chemistry.chemical_compound Transmembrane domain chemistry Membrane protein Mitochondrial Membranes Carbonate Amino Acid Sequence skin and connective tissue diseases Inner mitochondrial membrane Hydrophobic and Hydrophilic Interactions Molecular Biology Integral membrane protein |
| Zdroj: | Protein Science. 24:2063-2069 |
| ISSN: | 1469-896X 0961-8368 |
| DOI: | 10.1002/pro.2817 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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