De novo determination of protein backbone structure from residual dipolar couplings using Rosetta.

By Carol A. Rohl, David Baker. 2002

177 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. Oliver F. Lange
2. Gaetano T. Montelione
3. Julia Koehler Leman
4. Yuanpeng Janet Huang
5. J. Aramini
6. Jens Meiler
7. Richard Bonneau
8. Georg Kuenze

In Molecular Biology

1. Oliver F. Lange
2. Gaetano T. Montelione
3. Julia Koehler Leman
4. Jens Meiler
5. Yuanpeng Janet Huang
6. Richard Bonneau
7. J. Aramini
8. Georg Kuenze

Citations in the corpus

• Practically Useful: What the Rosetta Protein Modeling Suite Can Do for You (2010, methodology): “Rohl and Baker ( 35 ) likewise demonstrated that limited RDC measurements (approximately one per residue) in combination with backbone chemical shifts identify the correct fold.”
• Rosetta FunFolDes – A general framework for the computational design of functional proteins (2018, background): “Furthermore, FunFolDes is no longer limited to atom-pair distance constraints (Rohl & Baker, 2002) and can incorporate other types of kinematic constraints, such as angle and dihedral constraints (Bowers, Strauss, & Baker, 2000), which have been used to improve success rates when folding scaffolds…”
• Integrative protein modeling in RosettaNMR from sparse paramagnetic restraints (2019, methodology): “This method was later expanded to leverage RDCs from conventional (non-paramagnetic) alignment media (Rohl and Baker, 2002).”
• Machine Learning Methods for Protein Structure Prediction (2008, unknown): “[83]–[85] or protein structure determination by NMR methods.”
• Automated protein fold determination using a minimal NMR constraint strategy (2003, methodology): “In fact, RDC data have been used as primary NMR constraints for rapid determination of protein global folds (Delaglio et al. 2000; Fowler et al. 2000; Hus et al. 2000; Andrec et al. 2001, 2002; Rohl and Baker 2002).”
• Automatic NOESY assignment in CS-RASREC-Rosetta (2014, background): “Restraints with a high sequence can frustrate sampling in Rosetta fragment assembly considerably (Rohl and Baker 2002).”
• Local Protein Structures (2007, methodology): “Rosetta method has been extended to other protein modelling problems like de novo protein design [341, 342], protein-protein docking [343], protein modelling based on limited experimental data [344, 345] and loop modelling or modelling structurally variable regions in homologous proteins [346].”