ArticleProtein science : a publication of the Protein Society2003
Automated protein fold determination using a minimal NMR constraint strategy.
Article in Protein science : a publication of the Protein Society, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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29 citing papers in PubMed.
- Article
- Critical assessment of methods of protein structure prediction: Progress and new directions in round XI.Proteins · 2016Article
- A community resource of experimental data for NMR / X-ray crystal structure pairs.Protein science : a publication of the Protein Society · 2016Review
- Article
- Article
- A unified NMR strategy for high-throughput determination of backbone fold of small proteins.Journal of structural and functional genomics · 2012Article
- High resolution methyl selective ¹³C-NMR of proteins in solution and solid state.Journal of biomolecular NMR · 2012Article
- Protein side-chain resonance assignment and NOE assignment using RDC-defined backbones without TOCSY data.Journal of biomolecular NMR · 2011Article
- Preparation of protein samples for NMR structure, function, and small-molecule screening studies.Methods in enzymology · 2011Article
- A novel strategy for NMR resonance assignment and protein structure determination.Journal of biomolecular NMR · 2011Article
- Fully automated high-quality NMR structure determination of small (2)H-enriched proteins.Journal of structural and functional genomics · 2010Article
- High-resolution methyl edited GFT NMR experiments for protein resonance assignments and structure determination.Journal of biomolecular NMR · 2010Article
- Efficient condensed-phase production of perdeuterated soluble and membrane proteins.Journal of structural and functional genomics · 2010Article
- Advances in protein NMR provided by the NIGMS Protein Structure Initiative: impact on drug discovery.Current opinion in drug discovery & development · 2010Review
- Structure-oriented methods for protein NMR data analysis.Progress in nuclear magnetic resonance spectroscopy · 2010Review
- NMR structure determination for larger proteins using backbone-only data.Science (New York, N.Y.) · 2010Article
- Methyl groups as probes of supra-molecular structure, dynamics and function.Journal of biomolecular NMR · 2010Review
- Synergy of NMR, computation, and X-ray crystallography for structural biology.Structure (London, England : 1993) · 2009Article
- Unique opportunities for NMR methods in structural genomics.Journal of structural and functional genomics · 2009Article
- Raf kinase inhibitory protein function is regulated via a flexible pocket and novel phosphorylation-dependent mechanism.Molecular and cellular biology · 2009Article
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7 authors.
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Abstract
Determination of precise and accurate protein structures by NMR generally requires weeks or even months to acquire and interpret all the necessary NMR data. However, even medium-accuracy fold information can often provide key clues about protein evolution and biochemical function(s). In this article we describe a largely automatic strategy for rapid determination of medium-accuracy protein backbone structures. Our strategy derives from ideas originally introduced by other groups for determining medium-accuracy NMR structures of large proteins using deuterated, (13)C-, (15)N-enriched protein samples with selective protonation of side-chain methyl groups ((13)CH(3)). Data collection includes acquiring NMR spectra for automatically determining assignments of backbone and side-chain (15)N, H(N) resonances, and side-chain (13)CH(3) methyl resonances. These assignments are determined automatically by the program AutoAssign using backbone triple resonance NMR data, together with Spin System Type Assignment Constraints (STACs) derived from side-chain triple-resonance experiments. The program AutoStructure then derives conformational constraints using these chemical shifts, amide (1)H/(2)H exchange, nuclear Overhauser effect spectroscopy (NOESY), and residual dipolar coupling data. The total time required for collecting such NMR data can potentially be as short as a few days. Here we demonstrate an integrated set of NMR software which can process these NMR spectra, carry out resonance assignments, interpret NOESY data, and generate medium-accuracy structures within a few days. The feasibility of this combined data collection and analysis strategy starting from raw NMR time domain data was illustrated by automatic analysis of a medium accuracy structure of the Z domain of Staphylococcal protein A.
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