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Buried hydrophobic side-chains essential for the folding of the parallel β-helix domains of the P22 tailspike
The processive β-strands and turns of a polypeptide parallel β-helix represent one of the topologically simplest β-sheet folds. The three subunits of the tailspike adhesin of phage P22 each contain 13 rungs of a parallel β-helix followed by an interdigitated section of triple-stranded β-helix. Long...
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| Autori principali: | , , , |
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| Natura: | Artigo |
| Lingua: | Inglês |
| Pubblicazione: |
Cold Spring Harbor Laboratory Press
2004
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| Soggetti: | |
| Accesso online: | https://ncbi.nlm.nih.gov/pmc/articles/PMC2280027/ https://ncbi.nlm.nih.gov/pubmed/15322277 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1110/ps.04676704 |
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