| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 10797633 | Biochimica et Biophysica Acta (BBA) - Biomembranes | 2011 | 8 Pages |
Abstract
⺠Unfolding and refolding LamB protein in detergent exhibits extreme hysteresis. ⺠Without its disulfide bond, LamB protein unfolds in low denaturant concentrations. ⺠The disulfide bond clasps the sides of L1 at the inner wall of the β-barrel. ⺠Low pH dissociates the LamB trimer to folded monomers, observable on SDS PAGE. ⺠Low pH disrupts salt bridges between L2 of the adjacent subunit and the β- barrel.
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Authors
Valerie Baldwin, Mandeep Bhatia, Mary Luckey,