Solution NMR-derived global fold of a monomeric 82-kDa enzyme.

By V. Tugarinov, Wing Yiu Choy, V. Orekhov, Lewis E. Kay. 2005

211 citations recorded by the source corpus.

Subfields: Materials Chemistry, Molecular Biology

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

1. A. Bax
2. Yang Shen
3. Gabriel Cornilescu
4. A. Grishaev
5. Jill Trewhella
6. Lewis E. Kay
7. V. Tugarinov
8. Woonghee Lee

In Molecular Biology

1. A. Bax
2. Yang Shen
3. Gabriel Cornilescu
4. Jill Trewhella
5. Nikolaos G. Sgourakis
6. Santrupti Nerli
7. Woonghee Lee
8. John L. Markley

Citations in the corpus

• Refined solution structure of the 82-kDa enzyme malate synthase G from joint NMR and synchrotron SAXS restraints (2008, methodology): “45) were used, equal to those in the earlier NMR-only study (Tugarinov et al. 2005).”
• 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).”