ArticleJournal of biomolecular NMR2015
An optimized method for (15)N R(1) relaxation rate measurements in non-deuterated proteins.
Article in Journal of biomolecular NMR, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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12 citing papers in PubMed, 20 citations in OpenAlex.
- Gel-Based NMR Method for Observing Submicrosecond Protein Dynamics at Atomic Resolution.The journal of physical chemistry letters · 2026Article
- Detection of intramolecular protein dynamics on nanosecond-to-microsecond timescales by nanoparticle-assisted NMR spin relaxation (NASR).Nature protocols · 2026Review
- Pitfalls in measurements of RJournal of biomolecular NMR · 2025Article
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- Modulation of peroxisomal import by the PEX13 SH3 domain and a proximal FxxxF binding motif.Nature communications · 2024Article
- Excited-state observation of active K-Ras reveals differential structural dynamics of wild-type versus oncogenic G12D and G12C mutants.Nature structural & molecular biology · 2023Article
- Histone H4 Tails in Nucleosomes: a Fuzzy Interaction with DNA.Angewandte Chemie (International ed. in English) · 2021Article
- Functional protein dynamics on uncharted time scales detected by nanoparticle-assisted NMR spin relaxation.Science advances · 2019Article
- What DrivesBiophysical journal · 2018Article
- TROSY pulse sequence for simultaneous measurement of theJournal of biomolecular NMR · 2018Article
- Quantifying protein dynamics in the ps-ns time regime by NMR relaxation.Journal of biomolecular NMR · 2016Article
- Rapid Determination of Fast Protein Dynamics from NMR Chemical Exchange Saturation Transfer Data.Angewandte Chemie (International ed. in English) · 2016Article
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6 authors at 2 institutions in 1 country.
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Abstract
(15)N longitudinal relaxation rates are extensively used for the characterization of protein dynamics; however, their accurate measurement is hindered by systematic errors. (15)N CSA/(1)H-(15)N dipolar cross-correlated relaxation (CC) and amide proton exchange saturation transfer from water protons are the two main sources of systematic errors in the determination of (15)N R1 rates through (1)H-(15)N HSQC-based experiments. CC is usually suppressed through a train of 180° proton pulses applied during the variable (15)N relaxation period (T), which can perturb water magnetization. Thus CC cancellation is required in such a way as to minimize water saturation effects. Here we examined the level of water saturation during the T period caused by various types of inversion proton pulses to suppress CC: (I) amide-selective IBURP-2; (II) cosine-modulated IBURP-2; (III) Watergate-like blocks; and (IV) non-selective hard. We additionally demonstrate the effect of uncontrolled saturation of aliphatic protons on (15)N R1 rates. In this paper we present an optimized pulse sequence that takes into account the crucial effect of controlling also the saturation of the aliphatic protons during (15)N R1 measurements in non-deuterated proteins. We show that using cosine-modulated IBURP-2 pulses spaced 40 ms to cancel CC in this optimized pulse program is the method of choice to minimize systematic errors coming from water and aliphatic protons saturation effects.
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