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Residual Dipolar Couplings for Resolving Cysteine Bridges in Disulfide-Rich Peptides
Disulfide bridges in proteins are formed by the oxidation of pairs of cysteine residues. These cross-links play a critical role in stabilizing the 3D-structure of small disulfide rich polypeptides such as hormones and venom toxins. The arrangement of the multiple disulfide bonds directs the peptide...
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| 出版年: | Front Chem |
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| 主要な著者: | , , , |
| フォーマット: | Artigo |
| 言語: | Inglês |
| 出版事項: |
Frontiers Media S.A.
2020
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| 主題: | |
| オンライン･アクセス: | https://ncbi.nlm.nih.gov/pmc/articles/PMC6987419/ https://ncbi.nlm.nih.gov/pubmed/32039137 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.3389/fchem.2019.00889 |
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