| Chapter title |
Assessing the Outer Membrane Insertion and Folding of Multimeric Transmembrane β-Barrel Proteins
|
|---|---|
| Chapter number | 12 |
| Book title |
The BAM Complex
|
| Published in |
Methods in molecular biology, January 2015
|
| DOI | 10.1007/978-1-4939-2871-2_12 |
| Pubmed ID | |
| Book ISBNs |
978-1-4939-2870-5, 978-1-4939-2871-2
|
| Authors |
Jack C. Leo, Philipp Oberhettinger, Dirk Linke, Leo, Jack C., Oberhettinger, Philipp, Linke, Dirk |
| Abstract |
In addition to the cytoplasmic membrane, Gram-negative bacteria have a second lipid bilayer, the outer membrane, which is the de facto barrier between the cell and the extracellular milieu. Virtually all integral proteins of the outer membrane form β-barrels, which are inserted into the outer membrane by the BAM complex. Some outer membrane proteins, like the porins and trimeric autotransporter adhesins, are multimeric. In the former case, the porin trimer consists of three individual β-barrels, whereas in the latter, the single autotransporter β-barrel domain is formed by three separate polypeptides. This chapter reviews methods to investigate the folding and membrane insertion of multimeric OMPs and further explains the use of a BamA depletion strain to study the effects of the BAM complex on multimeric OMPs in E. coli. |
Mendeley readers
Geographical breakdown
| Country | Count | As % |
|---|---|---|
| Unknown | 9 | 100% |
Demographic breakdown
| Readers by professional status | Count | As % |
|---|---|---|
| Student > Ph. D. Student | 5 | 56% |
| Student > Doctoral Student | 1 | 11% |
| Unknown | 3 | 33% |
| Readers by discipline | Count | As % |
|---|---|---|
| Biochemistry, Genetics and Molecular Biology | 6 | 67% |
| Unknown | 3 | 33% |