ArticleJournal of magnetic resonance (San Diego, Calif. : 1997)2016
ARTSY-J: Convenient and precise measurement of (3)JHNHα couplings in medium-size proteins from TROSY-HSQC spectra.
Article in Journal of magnetic resonance (San Diego, Calif. : 1997), 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed.
- Microsecond Backbone Motions Modulate the Oligomerization of the DNAJB6 Chaperone.Angewandte Chemie (International ed. in English) · 2022Article
- Microsecond Backbone Motions Modulate the Oligomerization of the DNAJB6 Chaperone.Angewandte Chemie (Weinheim an der Bergstrasse, Germany) · 2022Article
- Structural Analysis of the Menangle Virus P Protein Reveals a Soft Boundary between Ordered and Disordered Regions.Viruses · 2021Article
- Remarkable Rigidity of the Single α-Helical Domain of Myosin-VI As Revealed by NMR Spectroscopy.Journal of the American Chemical Society · 2019Article
- Modern Technologies of Solution Nuclear Magnetic Resonance Spectroscopy for Three-dimensional Structure Determination of Proteins Open Avenues for Life Scientists.Computational and structural biotechnology journal · 2017Review
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Authors and funding
5 authors.
Funding
Abstract
A new and convenient method, named ARTSY-J, is introduced that permits extraction of the (3)JHNHα couplings in proteins from the relative intensities in a pair of (15)N-(1)H TROSY-HSQC spectra. The pulse scheme includes (3)JHNHα dephasing of the narrower TROSY (1)H(N)-{(15)N} doublet component during a delay, integrated into the regular two-dimensional TROSY-HSQC pulse scheme, and compares the obtained intensity with a reference spectrum where (3)JHNHα dephasing is suppressed. The effect of passive (1)H(α) spin flips downscales the apparent (3)JHNHα coupling by a uniform factor that depends approximately linearly on both the duration of the (3)JHNHα dephasing delay and the (1)H-(1)H cross relaxation rate. Using such a correction factor, which accounts for the effects of both inhomogeneity of the radiofrequency field and (1)H(α) spin flips, agreement between prior and newly measured values for the small model protein GB3 is better than 0.3Hz. Measurement for the HIV-1 protease homodimer (22kDa) yields (3)JHNHα values that agree to better than 0.7Hz with predictions made on the basis of a previously parameterized Karplus equation. Although for Gly residues the two individual (3)JHNHα couplings cannot be extracted from a single set of ARTSY-J spectra, the measurement provides valuable ϕ angle information.
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