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Structure and disorder in the ribonuclease S-peptide probed by NMR residual dipolar couplings
NMR residual dipolar couplings for the S-peptide of ribonuclease A aligned in C8E5/n-octanol liquid crystals are consistent with the presence of a native-like α-helix structure undergoing dynamic fraying. Residues 3–13, which correspond to the first α-helix of ribonuclease A, show couplings that bec...
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| Asıl Yazarlar: | , |
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| Materyal Türü: | Artigo |
| Dil: | Inglês |
| Baskı/Yayın Bilgisi: |
Cold Spring Harbor Laboratory Press
2003
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| Konular: | |
| Online Erişim: | https://ncbi.nlm.nih.gov/pmc/articles/PMC2366913/ https://ncbi.nlm.nih.gov/pubmed/14500871 |
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