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Optimal isotope labelling for NMR protein structure determinations
- Source :
- Nature. 440:52-57
- Publication Year :
- 2006
- Publisher :
- Springer Science and Business Media LLC, 2006.
-
Abstract
- Nuclear-magnetic-resonance spectroscopy can determine the three-dimensional structure of proteins in solution. However, its potential has been limited by the difficulty of interpreting NMR spectra in the presence of broadened and overlapping resonance lines and low signal-to-noise ratios. Here we present stereo-array isotope labelling (SAIL), a technique that can overcome many of these problems by applying a complete stereospecific and regiospecific pattern of stable isotopes that is optimal with regard to the quality and information content of the resulting NMR spectra. SAIL uses exclusively chemically and enzymatically synthesized amino acids for cell-free protein expression. We demonstrate for the 17-kDa protein calmodulin and the 41-kDa maltodextrin-binding protein that SAIL offers sharpened lines, spectral simplification without loss of information, and the ability to rapidly collect the structural restraints required to solve a high-quality solution structure for proteins twice as large as commonly solved by NMR. It thus makes a large class of proteins newly accessible to detailed solution structure determination.
- Subjects :
- Models, Molecular
Calmodulin
Crystallography, X-Ray
Protein structure
Labelling
Amino Acids
Spectroscopy
Nuclear Magnetic Resonance, Biomolecular
Multidisciplinary
biology
Chemistry
Stable isotope ratio
Escherichia coli Proteins
Proteins
Resonance
Cyana
Deuterium
biology.organism_classification
Carbon
Molecular Weight
NMR spectra database
Crystallography
Isotope Labeling
Periplasmic Binding Proteins
biology.protein
Carrier Proteins
Hydrogen
Subjects
Details
- ISSN :
- 14764687 and 00280836
- Volume :
- 440
- Database :
- OpenAIRE
- Journal :
- Nature
- Accession number :
- edsair.doi.dedup.....8c3a396383b2088bf7825fb869e810ec