ArticleJournal of biomolecular NMR2013
Fast hydrogen exchange affects ¹⁵N relaxation measurements in intrinsically disordered proteins.
Article in Journal of biomolecular NMR, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed.
- In-Cell Residue-Resolved NMR of Micromolar α-Synuclein and Tau at 310 K.Journal of the American Chemical Society · 2025Article
- NMR methods for investigating functionally relevant biomolecular dynamics.Magnetic resonance letters · 2025Review
- Cross-Polarization of Insensitive Nuclei from Water Protons for Detection of Protein-Ligand Binding.Journal of the American Chemical Society · 2024Article
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- Dynamics in natural and designed elastins and their relation to elastic fiber structure and recoil.Biophysical journal · 2021Article
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- Equilibrium folding dynamics of meACP in water, heavy water, and low concentration of urea.Scientific reports · 2017Article
- Structural Basis of the High Affinity Interaction between the Alphavirus Nonstructural Protein-3 (nsP3) and the SH3 Domain of Amphiphysin-2.The Journal of biological chemistry · 2016Article
- Article
- Spectral density mapping protocols for analysis of molecular motions in disordered proteins.Journal of biomolecular NMR · 2014Article
- HN(CA)N and HN(COCA)N experiments for assignment of large disordered proteins.Journal of biomolecular NMR · 2013Article
- Structural characterization of intrinsically disordered proteins by NMR spectroscopy.Molecules (Basel, Switzerland) · 2013Review
- Digested disorder: Quarterly intrinsic disorder digest (January/February/March, 2013).Intrinsically disordered proteinsReview
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3 authors.
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Abstract
Unprotected amide protons can undergo fast hydrogen exchange (HX) with protons from the solvent. Generally, NMR experiments using the out-and-back coherence transfer with amide proton detection are affected by fast HX and result in reduced signal intensity. When one of these experiments, (1)H-(15)N HSQC, is used to measure the (15)N transverse relaxation rate (R2), the measured R2 rate is convoluted with the HX rate (kHX) and has higher apparent R2 values. Since the (15)N R2 measurement is important for analyzing protein backbone dynamics, the HX effect on the R2 measurement is investigated and described here by multi-exponential signal decay. We demonstrate these effects by performing (15)N R 2 (CPMG) experiments on α-synuclein, an intrinsically disordered protein, in which the amide protons are exposed to solvent. We show that the HX effect on R 2 (CPMG) can be extracted by the derived equation. In conclusion, the HX effect may be pulse sequence specific and results from various sources including the J coupling evolution, the change of steady state water proton magnetization, and the D2O content in the sample. To avoid the HX effect on the analysis of relaxation data of unprotected amides, it is suggested that NMR experimental conditions insensitive to the HX should be considered or that intrinsic R 2 (CPMG) values be obtained by methods described herein.
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