Refined solution structure of the 82-kDa enzyme malate synthase G from joint NMR and synchrotron SAXS restraints
By A. Grishaev, V. Tugarinov, Lewis E. Kay, Jill Trewhella, A. Bax. 2008
113 citations recorded by the source corpus.
Subfields: Materials Chemistry, Molecular Biology, Spectroscopy
How researchers see this paper
The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.
In Materials Chemistry
- Andriy Kryshtafovych
- Torsten Schwede
- Krzysztof Fidelis
- Anna Tramontano
- John Moult
- Yang Zhang
- Bohdan Monastyrskyy
- Gaetano T. Montelione
In Molecular Biology
- Andriy Kryshtafovych
- Torsten Schwede
- Krzysztof Fidelis
- Anna Tramontano
- Yang Zhang
- John Moult
- Bohdan Monastyrskyy
- Gaetano T. Montelione
In Spectroscopy
- Andriy Kryshtafovych
- Krzysztof Fidelis
- Anna Tramontano
- Torsten Schwede
- John Moult
- Yang Shen
- A. Bax
- Gabriel Cornilescu
Citations in the corpus
- Critical Assessment of Methods of Protein Structure Prediction (CASP) – Progress and New directions in Round XI (2016, background): “27–31 However, perdeuteration also reduces the number of 1 H-1 H NOE-based distance restraints that can be obtained, providing models that are less accurate and precise, and in many cases precluding structure determination by conventional NMR structural modeling techniques alto-gether.”
- Protein structure determination by combining sparse NMR data with evolutionary couplings (2015, unknown): “Such “sparse NMR data” can generally be obtained for perdeuterated proteins with molecular weights as large as 40– 60 kDa 22–24 , and have been used in exceptional cases to determine chain folds for proteins as large as 82 kDa 25,26 .”
- TALOS+: A hybrid method for predicting protein backbone torsion angles from NMR chemical shifts (2009, background): “3 Å C rmsd) when the new TALOS? restraints are included instead of the TALOS restraints used originally (Tugarinov et al. 2005; Grishaev et al. 2008).”