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...

Täydet tiedot

Tallennettuna:
Bibliografiset tiedot
Päätekijät: Traaseth, Nathaniel J., Chao, Fa-An, Masterson, Larry R., Mangia, Silvia, Garwood, Michael, Michaeli, Shalom, Seelig, Burckhard, Veglia, Gianluigi
Aineistotyyppi: Artigo
Kieli:Inglês
Julkaistu: 2012
Aiheet:
Article
Linkit: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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