The solid-state proton-driven spin diffusion (PDSD) and J-decoupled PDSD NMR spectra of the microcrystalline catalytic domain of matrix metalloproteinase 12 (MMP-12, 17 kDa) have been recorded. It is shown that such spectra can be largely assigned in a few days by using the available liquid-state assignment and validated with an independent sequential assignment based on 3D NCACX and NCOCX PDSD experiments. This demonstrates how quickly the liquid-state assignment of comparably large protein can be transferred to the solid state.
Solid-state NMR of matrix metalloproteinase 12: An approach complementary to solution NMR / S. Balayssac; I. Bertini; K. Falber; M. Fragai; S. Jehle; M. Lelli; C. Luchinat; H. Oschkinat; K. J. Yeo. - In: CHEMBIOCHEM. - ISSN 1439-4227. - STAMPA. - 8:(2007), pp. 486-489. [10.1002/cbic.200600408]
Solid-state NMR of matrix metalloproteinase 12: An approach complementary to solution NMR
BERTINI, IVANO;FRAGAI, MARCO;LELLI, MORENOWriting – Original Draft Preparation
;LUCHINAT, CLAUDIO;YEO, KWON JOO
2007
Abstract
The solid-state proton-driven spin diffusion (PDSD) and J-decoupled PDSD NMR spectra of the microcrystalline catalytic domain of matrix metalloproteinase 12 (MMP-12, 17 kDa) have been recorded. It is shown that such spectra can be largely assigned in a few days by using the available liquid-state assignment and validated with an independent sequential assignment based on 3D NCACX and NCOCX PDSD experiments. This demonstrates how quickly the liquid-state assignment of comparably large protein can be transferred to the solid state.File | Dimensione | Formato | |
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