| Chapter title |
The Structure-Forming Juncture in Oxidative Protein Folding: What Happens in the ER?
|
|---|---|
| Chapter number | 88 |
| Book title |
Protein Reviews
|
| Published in |
Advances in experimental medicine and biology, January 2017
|
| DOI | 10.1007/5584_2017_88 |
| Pubmed ID | |
| Book ISBNs |
978-9-81-106921-5, 978-9-81-106922-2
|
| Authors |
Mahesh Narayan, Narayan, Mahesh |
| Abstract |
The folding of disulfide bond containing proteins proceeds in a biphasic manner. Initially, cysteines are oxidized to form disulfide bonds. Structure is largely absent during this phase. Next, when a minimally correct number of native linkages of disulfide bonds have been acquired, the biopolymer conformationally folds into the native, or a native-like, state. Thus, at the end of this "oxidative folding" process, a stable and biologically active protein is formed. This review focuses on dissecting the "structure-forming step" in oxidative protein folding. The ability to follow this pivotal step in protein maturation in somewhat detail is uniquely facilitated in "oxidative" folding scenarios. We review this step using bovine pancreatic Ribonuclease A as a model while recognizing the impact that this step has in subcellular trafficking and protein aggregation. |
Mendeley readers
Geographical breakdown
| Country | Count | As % |
|---|---|---|
| Unknown | 5 | 100% |
Demographic breakdown
| Readers by professional status | Count | As % |
|---|---|---|
| Student > Ph. D. Student | 2 | 40% |
| Researcher | 1 | 20% |
| Unknown | 2 | 40% |
| Readers by discipline | Count | As % |
|---|---|---|
| Biochemistry, Genetics and Molecular Biology | 1 | 20% |
| Neuroscience | 1 | 20% |
| Unknown | 3 | 60% |