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Disulfide-mediated beta strand dimers: hyperstable beta sheets lacking tertiary interactions and turns
Disulfide bonds between cysteine residues are essential to the structure and folding of many proteins. Yet their role in the design of structured peptides and proteins has frequently been limited to use as intra-chain covalent staples that reinforce existing structure or induce knot-like conformatio...
Gorde:
| Argitaratua izan da: | J Am Chem Soc |
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| Egile Nagusiak: | , , |
| Formatua: | Artigo |
| Hizkuntza: | Inglês |
| Argitaratua: |
2015
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| Gaiak: | |
| Sarrera elektronikoa: | https://ncbi.nlm.nih.gov/pmc/articles/PMC7450586/ https://ncbi.nlm.nih.gov/pubmed/25835058 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1021/ja5117809 |
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