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Heteronuclear Adiabatic Relaxation Dispersion (HARD) for quantitative analysis of conformational dynamics in proteins
NMR relaxation methods probe biomolecular motions over a wide range of timescales. In particular, the rotating frame spin-lock R(1)(ρ) and Carr–Purcell–Meiboom–Gill (CPMG) R(2) experiments are commonly used to characterize μs to ms dynamics, which play a critical role in enzyme folding and catalysis...
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| Autori principali: | , , , , , , , |
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| Natura: | Artigo |
| Lingua: | Inglês |
| Pubblicazione: |
2012
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| Soggetti: | |
| Accesso online: | https://ncbi.nlm.nih.gov/pmc/articles/PMC3568944/ https://ncbi.nlm.nih.gov/pubmed/22621977 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1016/j.jmr.2012.03.024 |
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