ArticleJournal of biomolecular NMR2005
Accurate determination of leucine and valine side-chain conformations using U-[15N/13C/2H]/[1H-(methine/methyl)-Leu/Val] isotope labeling, NOE pattern recognition, and methine Cgamma-Hgamma/Cbeta-Hbeta residual dipolar couplings: application to the 34-kDa enzyme IIA(chitobiose).
Article in Journal of biomolecular NMR, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- Determining methyl sidechain conformations in a CS-ROSETTA model using methylJournal of biomolecular NMR · 2020Article
- CH3-specific NMR assignment of alanine, isoleucine, leucine and valine methyl groups in high molecular weight proteins using a single sample.Journal of biomolecular NMR · 2015Article
- The SARS coronavirus nucleocapsid protein--forms and functions.Antiviral research · 2014Review
- Biosynthetically directed ²H labelling for stereospecific resonance assignments of glycine methylene groups.Journal of biomolecular NMR · 2013Article
- A simple biosynthetic method for stereospecific resonance assignment of prochiral methyl groups in proteins.Journal of biomolecular NMR · 2011Article
- Automated error-tolerant macromolecular structure determination from multidimensional nuclear Overhauser enhancement spectra and chemical shift assignments: improved robustness and performance of the PASD algorithm.Journal of biomolecular NMR · 2008Article
- A simple and reliable approach to docking protein-protein complexes from very sparse NOE-derived intermolecular distance restraints.Journal of biomolecular NMR · 2006Article
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3 authors.
Funding
Abstract
An isotope labeling scheme is described in which specific protonation of methine and methyl protons of leucine and valine is obtained on a 15N/13C labeled background with uniform deuteration of all other non-exchangeable protons. The presence of a protonated methine group has little effect on the favorable relaxation properties of the methyl protons of Leu and Val. This labeling scheme permits the rotameric state of leucine side-chains to be readily determined by simple inspection of the pattern of Hgamma(i)-H(N)(i) and Hgamma(i)-H(N)(i+1) NOEs in a 3D 15N-separated NOE spectrum free of complications arising from spectral overlap and spin-diffusion. In addition, one-bond residual dipolar couplings for the methine 13C-1H bond vectors of Leu and Val can be accurately determined from an intensity J-modulated constant-time HCCH-COSY experiment and used to accurately orient the side-chains of Leu and Val. Incorporation of these data into structure refinement improves the accuracy with which the conformations of Leu and Val side-chains can be established. This is important to ensure optimal packing both within the protein core and at intermolecular interfaces. The impact of the method on protein structure determination is illustrated by application to enzyme IIA(Chitobiose), a 34 kDa homotrimeric phosphotransferase protein.
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