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Deuterated Protein Folds Obtained Directly from Unassigned NOE Data
We demonstrate the feasibility of determining the global fold of a highly deuterated protein from unassigned experimental NMR nuclear Overhauser effect (NOE) data only. The method relies on the calculation of a spatial configuration of covalently unconnected protons—a “cloud”—directly from unassigne...
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| Udgivet i: | J Am Chem Soc |
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| Main Authors: | , |
| Format: | Artigo |
| Sprog: | Inglês |
| Udgivet: |
2008
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| Fag: | |
| Online adgang: | https://ncbi.nlm.nih.gov/pmc/articles/PMC4819401/ https://ncbi.nlm.nih.gov/pubmed/18318535 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1021/ja074836e |
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