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

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 and secon...

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Veröffentlicht in:	Journal of the American Chemical Society 2004-12, Vol.126 (50), p.16608-16620
Hauptverfasser:	MARULANDA, Dabeiba, TASAYCO, Maria Luisa, MCDERMOTT, Ann, CATALDI, Marcela, ARRIARAN, Vilma, POLENOVA, Tatyana
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Analytical, structural and metabolic biochemistry Biological and medical sciences Carbon Isotopes Escherichia coli Proteins - chemistry Fundamental and applied biological sciences. Psychology General aspects, investigation methods Models, Molecular Molecular Sequence Data Nitrogen Isotopes Nuclear Magnetic Resonance, Biomolecular - methods Peptide Fragments - chemistry Polyethylene Glycols - chemistry Proteins Thioredoxins - chemistry
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