ReviewRSC advances2023
The influence of random-coil chemical shifts on the assessment of structural propensities in folded proteins and IDPs.
Review in RSC advances, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
3 citing papers in PubMed.
- A Data Set of Simple 1-D and 2-D NMR Spectra of Peptides, including All Encoded Amino Acids, for Introductory Instruction in Protein Biomolecular NMR Spectroscopy.Biochemistry · 2026Article
- DR and SPIT: Statistical approaches for identifying transient structure in intrinsically disordered proteins via NMR chemical shifts.Protein science : a publication of the Protein Society · 2025Article
- A computational approach to design a multiepitope vaccine against H5N1 virus.Virology journal · 2024Article
Corrections and comments
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Authors and funding
2 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In studying secondary structural propensities of proteins by nuclear magnetic resonance (NMR) spectroscopy, secondary chemical shifts (SCSs) serve as the primary atomic scale observables. For SCS calculation, the selection of an appropriate random coil chemical shift (RCCS) dataset is a crucial step, especially when investigating intrinsically disordered proteins (IDPs). The scientific literature is abundant in such datasets, however, the effect of choosing one over all the others in a concrete application has not yet been studied thoroughly and systematically. Hereby, we review the available RCCS prediction methods and to compare them, we conduct statistical inference by means of the nonparametric sum of ranking differences and comparison of ranks to random numbers (SRD-CRRN) method. We try to find the RCCS predictors best representing the general consensus regarding secondary structural propensities. The existence and the magnitude of resulting differences on secondary structure determination under varying sample conditions (temperature, pH) are demonstrated and discussed for globular proteins and especially IDPs.
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Registered trials
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