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Conformational exchange of aromatic side chains characterized by L-optimized TROSY-selected (13)C CPMG relaxation dispersion
Protein dynamics on the millisecond time scale commonly reflect conformational transitions between distinct functional states. NMR relaxation dispersion experiments have provided important insights into biologically relevant dynamics with site-specific resolution, primarily targeting the protein bac...
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| Main Authors: | , , |
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| Format: | Artigo |
| Sprog: | Inglês |
| Udgivet: |
Springer Netherlands
2012
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| Fag: | |
| Online adgang: | https://ncbi.nlm.nih.gov/pmc/articles/PMC3427480/ https://ncbi.nlm.nih.gov/pubmed/22833056 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1007/s10858-012-9656-z |
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