ArticleMethods in enzymology2005
Determination of protein backbone structures from residual dipolar couplings.
Article in Methods in enzymology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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Who cites it
32 citing papers in PubMed.
- Concurrent Identification and Characterization of Protein Structure and Continuous Internal Dynamics with REDCRAFT.Frontiers in molecular biosciences · 2022Article
- REDCRAFT: A computational platform using residual dipolar coupling NMR data for determining structures of perdeuterated proteins in solution.PLoS computational biology · 2021Article
- Simultaneous Assignment and Structure Determination of Proteins From Sparsely Labeled NMR Datasets.Frontiers in molecular biosciences · 2021Article
- On the complementarity of X-ray and NMR data.Journal of structural biology: X · 2020Article
- Improvements to REDCRAFT: a software tool for simultaneous characterization of protein backbone structure and dynamics from residual dipolar couplings.Journal of biomolecular NMR · 2014Article
- Simultaneous use of solution NMR and X-ray data in REFMAC5 for joint refinement/detection of structural differences.Acta crystallographica. Section D, Biological crystallography · 2014Article
- Sparse labeling of proteins: structural characterization from long range constraints.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2014Review
- Dynafold: a dynamic programming approach to protein backbone structure determination from minimal sets of Residual Dipolar Couplings.Journal of bioinformatics and computational biology · 2014Article
- Advances in the REDCAT software package.BMC bioinformatics · 2013Article
- Modeling helical proteins using residual dipolar couplings, sparse long-range distance constraints and a simple residue-based force field.Theoretical chemistry accounts · 2013Article
- Measuring dynamic and kinetic information in the previously inaccessible supra-τ(c) window of nanoseconds to microseconds by solution NMR spectroscopy.Molecules (Basel, Switzerland) · 2013Review
- Protein structure validation and identification from unassigned residual dipolar coupling data using 2D-PDPA.Molecules (Basel, Switzerland) · 2013Article
- The use of residual dipolar coupling in studying proteins by NMR.Topics in current chemistry · 2012Review
- Simultaneous structure and dynamics of a membrane protein using REDCRAFT: membrane-bound form of Pf1 coat protein.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2010Article
- Structure-oriented methods for protein NMR data analysis.Progress in nuclear magnetic resonance spectroscopy · 2010Review
- Advances in Nuclear Magnetic Resonance for Drug Discovery.Expert opinion on drug discovery · 2009Article
- Measurement of one and two bond N-C couplings in large proteins by TROSY-based J-modulation experiments.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2009Article
- Preparation of selective and segmentally labeled single-stranded DNA for NMR by self-primed PCR and asymmetrical endonuclease double digestion.Nucleic acids research · 2009Article
- Efficient and accurate estimation of relative order tensors from lambda-maps.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2009Article
- Automated structure determination from NMR spectra.European biophysics journal : EBJ · 2009Review
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4 authors.
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Abstract
There are a number of circumstances in which a focus on determination of the backbone structure of a protein, as opposed to a complete all-atom structure, may be appropriate. This is particularly the case for structures determined as a part of a structural genomics initiative in which computational modeling of many sequentially related structures from the backbone of a single family representative is anticipated. It is, however, also the case when the backbone may be a stepping-stone to more targeted studies of ligand interaction or protein-protein interaction. Here an NMR protocol is described that can produce a backbone structure of a protein without the need for extensive experiments directed at side chain resonance assignment or the collection of structural information on side chains. The procedure relies primarily on orientational constraints from residual dipolar couplings as opposed to distance constraints from NOEs. Procedures for sample preparation, data acquisition, and data analysis are described, along with examples from application to small target proteins of a structural genomics project.
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