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An optimized method for (15)N R(1) relaxation rate measurements in non-deuterated proteins
(15)N longitudinal relaxation rates are extensively used for the characterization of protein dynamics; however, their accurate measurement is hindered by systematic errors. (15)N CSA/(1)H–(15)N dipolar cross-correlated relaxation (CC) and amide proton exchange saturation transfer from water protons...
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| Pubblicato in: | J Biomol NMR |
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| Autori principali: | , , , , , |
| Natura: | Artigo |
| Lingua: | Inglês |
| Pubblicazione: |
Springer Netherlands
2015
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| Soggetti: | |
| Accesso online: | https://ncbi.nlm.nih.gov/pmc/articles/PMC4451471/ https://ncbi.nlm.nih.gov/pubmed/25947359 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1007/s10858-015-9937-4 |
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