Solid-state NMR of matrix metalloproteinase 12:: An approach complementary to solution NMR

被引:35
作者
Balayssac, Stephane
Bertini, Ivano
Faelber, Katja
Fragai, Marco
Jehle, Stefan
Lelli, Moreno
Luchinat, Claudio
Oschkinat, Hartmut
Yeo, Kwon Joo
机构
[1] Univ Florence, Magnet Resonance Ctr, CERM, I-50019 Sesto Fiorentino, Italy
[2] Univ Florence, Dept Chem, I-50019 Sesto Fiorentino, Italy
[3] Leibnizinst Mol Pharmakol, D-13125 Berlin, Germany
[4] Univ Florence, Dept Agr Biotechnol, I-50144 Florence, Italy
关键词
metalloproteinase; NMR spectroscopy; protein structures; solid-state NMR;
D O I
10.1002/cbic.200600408
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
(Figure Presented) Data transfer. 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. © 2007 Wiley-VCH Verlag GmbH & Co. KGaA.
引用
收藏
页码:486 / 489
页数:4
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