ArticleJournal of biomolecular NMR2009
Empirical correlation between protein backbone 15N and 13C secondary chemical shifts and its application to nitrogen chemical shift re-referencing.
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 19 papers.
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Who cites it
19 citing papers in PubMed.
- Predicted and Experimental NMR Chemical Shifts at Variable Temperatures: The Effect of Protein Conformational Dynamics.The journal of physical chemistry letters · 2024Review
- NMR-Based Characterization of the Interaction between Yeast Oxa1-CTD and Ribosomes.International journal of molecular sciences · 2023Article
- The influence of random-coil chemical shifts on the assessment of structural propensities in folded proteins and IDPs.RSC advances · 2023Review
- The residual structure of acid-denatured βProtein science : a publication of the Protein Society · 2023Article
- A transient α-helix in the N-terminal RNA recognition motif of polypyrimidine tract binding protein senses RNA secondary structure.Nucleic acids research · 2020Article
- Temperature dependence of NMR chemical shifts: Tracking and statistical analysis.Protein science : a publication of the Protein Society · 2020Article
- NMRFx Processor: a cross-platform NMR data processing program.Journal of biomolecular NMR · 2016Article
- Conformationally selective multidimensional chemical shift ranges in proteins from a PACSY database purged using intrinsic quality criteria.Journal of biomolecular NMR · 2016Article
- An overview of tools for the validation of protein NMR structures.Journal of biomolecular NMR · 2014Review
- Recommendations of the wwPDB NMR Validation Task Force.Structure (London, England : 1993) · 2013Article
- Vivaldi: visualization and validation of biomacromolecular NMR structures from the PDB.Proteins · 2013Article
- HASH: a program to accurately predict protein Hα shifts from neighboring backbone shifts.Journal of biomolecular NMR · 2013Article
- An automated system designed for large scale NMR data deposition and annotation: application to over 600 assigned chemical shift data entries to the BioMagResBank from the Riken Structural Genomics/Proteomics Initiative internal database.Journal of biomolecular NMR · 2012Article
- Combining NMR ensembles and molecular dynamics simulations provides more realistic models of protein structures in solution and leads to better chemical shift prediction.Journal of biomolecular NMR · 2012Article
- Orphan macrodomain protein (human C6orf130) is an O-acyl-ADP-ribose deacylase: solution structure and catalytic properties.The Journal of biological chemistry · 2011Article
- Time-resolved NMR: extracting the topology of complex enzyme networks.Biophysical journal · 2010Article
- A probabilistic approach for validating protein NMR chemical shift assignments.Journal of biomolecular NMR · 2010Article
- 4D prediction of protein (1)H chemical shifts.Journal of biomolecular NMR · 2009Article
- CheckShift improved: fast chemical shift reference correction with high accuracy.Journal of biomolecular NMR · 2009Article
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2 authors.
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Abstract
The linear analysis of chemical shifts (LACS) has provided a robust method for identifying and correcting 13C chemical shift referencing problems in data from protein NMR spectroscopy. Unlike other approaches, LACS does not require prior knowledge of the three-dimensional structure or inference of the secondary structure of the protein. It also does not require extensive assignment of the NMR data. We report here a way of extending the LACS approach to 15N NMR data from proteins, so as to enable the detection and correction of inconsistencies in chemical shift referencing for this nucleus. The approach is based on our finding that the secondary 15N chemical shift of the backbone nitrogen atom of residue i is strongly correlated with the secondary chemical shift difference (experimental minus random coil) between the alpha and beta carbons of residue i-1. Thus once alpha and beta 13C chemical shifts are available (their difference is referencing error-free), the 15N referencing can be validated, and an appropriate offset correction can be derived. This approach can be implemented prior to a structure determination and can be used to analyze potential referencing problems in database data not associated with three-dimensional structure. Application of the LACS algorithm to the current BMRB protein chemical shift database, revealed that nearly 35% of the BMRB entries have delta 15N values mis-referenced by over 0.7 ppm and over 25% of them have delta 1HN values mis-referenced by over 0.12 ppm. One implication of the findings reported here is that a backbone 15N chemical shift provides a better indicator of the conformation of the preceding residue than of the residue itself.
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