ArticleJournal of biomolecular NMR2009
Highly automated protein backbone resonance assignment within a few hours: the "BATCH" strategy and software package.
Article in Journal of biomolecular NMR, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- Amino acid recognition for automatic resonance assignment of intrinsically disordered proteins.Journal of biomolecular NMR · 2016Article
- Non-Uniform Sampling and J-UNIO Automation for Efficient Protein NMR Structure Determination.Chemistry (Weinheim an der Bergstrasse, Germany) · 2015Article
- APSY-NMR for protein backbone assignment in high-throughput structural biology.Journal of biomolecular NMR · 2015Article
- Parallel acquisition of 3D-HA(CA)NH and 3D-HACACO spectra.Journal of biomolecular NMR · 2013Article
- A unified NMR strategy for high-throughput determination of backbone fold of small proteins.Journal of structural and functional genomics · 2012Article
- New amino acid residue type identification experiments valid for protonated and deuterated proteins.Journal of biomolecular NMR · 2012Article
- The J-UNIO protocol for automated protein structure determination by NMR in solution.Journal of biomolecular NMR · 2012Article
- Rapid measurement of residual dipolar couplings for fast fold elucidation of proteins.Journal of biomolecular NMR · 2011Article
- AUTOBA: automation of backbone assignment from HN(C)N suite of experiments.Journal of biomolecular NMR · 2011Article
- Advances in Nuclear Magnetic Resonance for Drug Discovery.Expert opinion on drug discovery · 2009Article
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2 authors.
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Abstract
Sequential resonance assignment represents an essential step towards the investigation of protein structure, dynamics, and interaction surfaces. Although the experimental sensitivity has significantly increased in recent years, with the availability of high field magnets and cryogenically cooled probes, resonance assignment, even of small globular proteins, still generally requires several days of data collection and analysis using standard protocols. Here we introduce the BATCH strategy for fast and highly automated backbone resonance assignment of (13)C, (15)N-labelled proteins. BATCH makes use of the fast data acquisition and analysis tools BEST, ASCOM, COBRA, and HADAMAC, recently developed in our laboratory. An improved Hadamard encoding scheme, presented here, further increases the performance of the HADAMAC experiment. A new software platform, interfaced to the NMRView software package, has been developed that enables highly automated NMR data processing and analysis, sequential resonance assignment, and (13)C chemical shift extraction. We demonstrate for four small globular proteins that sequential resonance assignment can be routinely obtained within a few hours, or less, in a highly automated and robust way.
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