Structure of Fully Protonated Proteins by Proton-Detected Magic-Angle Spinning NMR
Proceedings of the National Academy of Sciences of the United States of America 2016
L.B. Andreas, Kristaps Jaudzems, J. Stanek, D. Lalli, A. Bertarello, T. Le Marchand, D. Cala-De Paepe, S. Kotelovica, I. Akopjana, B. Knott, S. Wegner, F. Engelke, A. Lesage, L. Emsley, K. Tars, T. Herrmann, G. Pintacuda

Protein structure determination is key to the detailed description of many biological processes. The critical factor that would allow general application of magic-angle spinning (MAS) solid-state NMR to this end is improvement in sensitivity and resolution for as many nuclear spins as possible. This is achieved here with detection of resolved 1H resonances in protonated proteins by increasing MAS rates to frequencies of 100 kHz and above. For large proteins and assemblies, ultrafast spinning narrows spectral resonances better than Brownian motion on which solution NMR relies, removing a fundamental barrier to the NMR study of large systems. This is exploited here to determine the de novo structure of a 28-kDa protein dimer in a 2.5-MDa viral capsid assembly.


Atslēgas vārdi
fully protonated proteins, proton-detected magic-angle spinning NMR.
DOI
10.1073/pnas.1602248113
Hipersaite
http://www.pnas.org/content/113/33/9187

Andreas, L., Jaudzems, K., Stanek, J., Lalli, D., Bertarello, A., Le Marchand, T., Cala-De Paepe, D., Kotelovica, S., Akopjana, I., Knott, B., Wegner, S., Engelke, F., Lesage, A., Emsley, L., Tars, K., Herrmann, T., Pintacuda, G. Structure of Fully Protonated Proteins by Proton-Detected Magic-Angle Spinning NMR. Proceedings of the National Academy of Sciences of the United States of America, 2016, Vol.113, No.33, 9187.-9192.lpp. e-ISSN 1091-6490. Pieejams: doi:10.1073/pnas.1602248113

Publikācijas valoda
English (en)
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