Optimized selection of slow-relaxing 13C transitions in methyl groups of proteins: application to relaxation dispersion.
J Biomol NMR
; 74(12): 673-680, 2020 Dec.
Article
em En
| MEDLINE
| ID: mdl-33006092
ABSTRACT
Optimized selection of the slow-relaxing components of single-quantum 13C magnetization in 13CH3 methyl groups of proteins using acute (< 90°) angle 1H radio-frequency pulses, is described. The optimal selection scheme is more relaxation-tolerant and provides sensitivity gains in comparison to the experiment where the undesired (fast-relaxing) components of 13C magnetization are simply 'filtered-out' and only 90° 1H pulses are employed for magnetization transfer to and from 13C nuclei. When applied to methyl 13C single-quantum Carr-Purcell-Meiboom-Gill (CPMG) relaxation dispersion experiments for studies of chemical exchange, the selection of the slow-relaxing 13C transitions results in a significant decrease in intrinsic (exchange-free) transverse spin relaxation rates of all exchanging species. For exchanging systems involving high-molecular-weight species, the lower transverse relaxation rates translate into an increase in the information content of the resulting relaxation dispersion profiles.
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Texto completo:
1
Bases de dados:
MEDLINE
Assunto principal:
Isótopos de Carbono
/
Proteínas
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Ressonância Magnética Nuclear Biomolecular
Idioma:
En
Revista:
J Biomol NMR
Assunto da revista:
BIOLOGIA MOLECULAR
/
DIAGNOSTICO POR IMAGEM
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MEDICINA NUCLEAR
Ano de publicação:
2020
Tipo de documento:
Article
País de afiliação:
Estados Unidos