ArticleJournal of biomolecular NMR2014
Pressure response of amide one-bond J-couplings in model peptides and proteins.
Article in Journal of biomolecular NMR, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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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.
- Solution NMR investigation of the response of the lactose repressor core domain dimer to hydrostatic pressure.Biophysical chemistry · 2017Article
- Pressure dependence of side chainJournal of biomolecular NMR · 2017Article
- Alternatives to Nuclear Overhauser Enhancement Spectroscopy Presat and Carr-Purcell-Meiboom-Gill Presat for NMR-Based Metabolomics.Analytical chemistry · 2017Article
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Authors and funding
7 authors.
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No grant is acknowledged in the PubMed record.
Abstract
The pressure dependence of the one-bond indirect spin-spin coupling constants (1)J(N-H) was studied in the protected tetrapeptides Ac-Gly-Gly-Xxx-Ala-NH2 (with Xxx being one of the 20 proteinogenic amino acids). The response of the (1)J(N-H) coupling constants is amino acid type specific, with an average increase of its magnitude by 0.6 Hz at 200 MPa. The variance of the pressure response is rather large, the largest pressure effect is observed for asparagine where the coupling constant becomes more negative by -2.9 Hz at 200 MPa. The size of the J-coupling constant at high pressure is positively correlated with its low pressure value and the β-propensity, and negatively correlated with the amide proton shift and the first order nitrogen pressure coefficient and the electrostatic solvation free energy.
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