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The leucine-rich repeat domain of Internalin B folds along a polarized N-terminal pathway
The leucine-rich repeat domain of Internalin B is composed of seven tandem leucine-rich repeats, which each contain a short β-strand connected to a 3(10)-helix by a short turn, and an N-terminal α-helical capping motif. To determine whether folding proceeds along a single discrete pathway or multipl...
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| Main Authors: | , |
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| Formáid: | Artigo |
| Teanga: | Inglês |
| Foilsithe: |
2008
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| Ábhair: | |
| Rochtain Ar Líne: | https://ncbi.nlm.nih.gov/pmc/articles/PMC2426962/ https://ncbi.nlm.nih.gov/pubmed/18462675 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1016/j.str.2008.02.015 |
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