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Slow ring flips in aromatic cluster of GB1 studied by aromatic (13)C relaxation dispersion methods
Ring flips of phenylalanine and tyrosine are a hallmark of protein dynamics. They report on transient breathing motions of proteins. In addition, flip rates also depend on stabilizing interactions in the ground state, like aromatic stacking or cation–π interaction. So far, experimental studies of ri...
Uloženo v:
| Vydáno v: | J Biomol NMR |
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| Hlavní autoři: | , , |
| Médium: | Artigo |
| Jazyk: | Inglês |
| Vydáno: |
Springer Netherlands
2020
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| Témata: | |
| On-line přístup: | https://ncbi.nlm.nih.gov/pmc/articles/PMC7080667/ https://ncbi.nlm.nih.gov/pubmed/32016706 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1007/s10858-020-00303-3 |
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