ArticleJournal of biomolecular NMR2005
A simple method to adjust inconsistently referenced 13C and 15N chemical shift assignments of proteins.
Article in Journal of biomolecular NMR, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed.
- Toward Accurate Simulation of Coupling between Protein Secondary Structure and Phase Separation.Journal of the American Chemical Society · 2024Article
- Developing Bonded Potentials for a Coarse-Grained Model of Intrinsically Disordered Proteins.Journal of chemical information and modeling · 2022Article
- Using NMR Chemical Shifts to Determine Residue-Specific Secondary Structure Populations for Intrinsically Disordered Proteins.Methods in enzymology · 2018Article
- Conformationally selective multidimensional chemical shift ranges in proteins from a PACSY database purged using intrinsic quality criteria.Journal of biomolecular NMR · 2016Article
- Peakmatch: a simple and robust method for peak list matching.Journal of biomolecular NMR · 2013Article
- A procedure to validate and correct the 13C chemical shift calibration of RNA datasets.Journal of biomolecular NMR · 2012Article
- Probing the self-association, intermolecular contacts, and folding propensity of amelogenin.Protein science : a publication of the Protein Society · 2011Article
- Article
- A probabilistic approach for validating protein NMR chemical shift assignments.Journal of biomolecular NMR · 2010Article
- CheckShift improved: fast chemical shift reference correction with high accuracy.Journal of biomolecular NMR · 2009Article
- Empirical correlation between protein backbone 15N and 13C secondary chemical shifts and its application to nitrogen chemical shift re-referencing.Journal of biomolecular NMR · 2009Article
- The tooth enamel protein, porcine amelogenin, is an intrinsically disordered protein with an extended molecular configuration in the monomeric form.Biochemistry · 2009Article
- Application of the random coil index to studying protein flexibility.Journal of biomolecular NMR · 2008Article
- CheckShift: automatic correction of inconsistent chemical shift referencing.Journal of biomolecular NMR · 2007Article
- Protein backbone chemical shifts predicted from searching a database for torsion angle and sequence homology.Journal of biomolecular NMR · 2007Article
- Sensitivity of secondary structure propensities to sequence differences between alpha- and gamma-synuclein: implications for fibrillation.Protein science : a publication of the Protein Society · 2006Article
- PREDITOR: a web server for predicting protein torsion angle restraints.Nucleic acids research · 2006Article
- Improving the accuracy of protein secondary structure prediction using structural alignment.BMC bioinformatics · 2006Article
Corrections and comments
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Authors and funding
2 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Inconsistent 13C and 15N chemical shift referencing is a continuing problem associated with protein chemical shift assignments deposited in BioMagResBank (BMRB). Here we describe a simple and robust approach that can quantitatively determine the 13C and 15N referencing offsets solely from chemical shift assignment data and independently of 3D coordinate data. This novel structure-independent approach permitted the assessment and determination of 13C and 15N reference offsets for all protein entries deposited in the BMRB. Tests on 452 proteins with known 3D structures show that this structure-independent approach yields 13C and 15N referencing offsets that exhibit excellent agreement with those calculated on the basis of 3D structures. Furthermore, this protocol appears to improve the accuracy of chemical shift-derived secondary structural identification, and has been formally incorporated into a computer program called PSSI (http//www.pronmr.com).
Indexed as
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15772753What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.