ArticleJournal of biomolecular NMR2001
Direct structure refinement of high molecular weight proteins against residual dipolar couplings and carbonyl chemical shift changes upon alignment: an application to maltose binding protein.
Article in Journal of biomolecular NMR, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed.
- Conformational Investigations in Flexible Molecules Using Orientational NMR Constraints in Combination withMolecules (Basel, Switzerland) · 2019Article
- Parameterization of solvent-protein interaction and its use on NMR protein structure determination.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2012Article
- Protein side-chain resonance assignment and NOE assignment using RDC-defined backbones without TOCSY data.Journal of biomolecular NMR · 2011Article
- Automated NMR Assignment and Protein Structure Determination using Sparse Dipolar Coupling Constraints.Progress in nuclear magnetic resonance spectroscopy · 2009Article
- Investigation of the utility of selective methyl protonation for determination of membrane protein structures.Journal of biomolecular NMR · 2008Article
- Refined solution structure of the 82-kDa enzyme malate synthase G from joint NMR and synchrotron SAXS restraints.Journal of biomolecular NMR · 2008Article
- Partial 13C isotopic enrichment of nucleoside monophosphates: useful reporters for NMR structural studies.Nucleic acids research · 2005Article
- Improving the accuracy of NMR structures of large proteins using pseudocontact shifts as long-range restraints.Journal of biomolecular NMR · 2004Article
- Application of correlated residual dipolar couplings to the determination of the molecular alignment tensor magnitude of oriented proteins and nucleic acids.Journal of biomolecular NMR · 2004Article
- Structure and disorder in the ribonuclease S-peptide probed by NMR residual dipolar couplings.Protein science : a publication of the Protein Society · 2003Article
- NMR structure of the forkhead-associated domain from the Arabidopsis receptor kinase-associated protein phosphatase.Proceedings of the National Academy of Sciences of the United States of America · 2003Article
- A novel strategy for the assignment of side-chain resonances in completely deuterated large proteins using 13C spectroscopy.Journal of biomolecular NMR · 2003Article
- Simultaneous measurement of protein one-bond and two-bond nitrogen-carbon coupling constants using an internally referenced quantitative J-correlated [(15)N,(1)H]-TROSY-HNC experiment.Journal of biomolecular NMR · 2003Article
- Structure-independent cross-validation between residual dipolar couplings originating from internal and external orienting media.Journal of biomolecular NMR · 2002Article
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Authors and funding
4 authors.
Funding
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Abstract
The global fold of maltose binding protein in complex with beta-cyclodextrin has been determined using a CNS-based torsion angle molecular dynamics protocol involving direct refinement against dipolar couplings and carbonyl chemical shift changes that occur upon alignment. The shift changes have been included as structural restraints using a new module, CANI, that has been incorporated into CNS. Force constants and timesteps have been determined that are particularly effective in structure refinement applications involving high molecular weight proteins with small to moderate numbers of NOE restraints. Solution structures of the N- and C-domains of MBP calculated with this new protocol are within approximately 2 A of the X-ray conformation.
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