Magic angle spinning solid-state NMR spectroscopy for structural studies of protein interfaces. resonance assignments of differentially enriched Escherichia coli thioredoxin reassembled by fragment complementation.
作者： Dabeiba Marulanda , Maria Luisa Tasayco , Ann McDermott , Marcela Cataldi , Vilma Arriaran
DOI: 10.1021/JA0464589
关键词: Nuclear magnetic resonance spectroscopy 、 Thioredoxin 、 Crystallography 、 Chemistry 、 Chemical shift 、 Magic angle spinning 、 Protein secondary structure 、 Solid-state nuclear magnetic resonance 、 Spectroscopy 、 Dihedral angle 、 Analytical chemistry
摘要: De novo site-specific backbone and side-chain resonance assignments are presented for U-15N(1−73)/U-13C,15N(74−108) reassembly of Escherichia coli thioredoxin by fragment complementation, determined using solid-state magic angle spinning NMR spectroscopy at 17.6 T. Backbone dihedral angles secondary structure predicted from the statistical analysis 13C 15N chemical shifts in general agreement with solution values intact full-length thioredoxin, confirming that is retained reassembled complex prepared as a poly(ethylene glycol) precipitate. The differential labeling complementary fragments introduced this work expected to be beneficial high-resolution structural studies protein interfaces formed assemblies spectroscopy.
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