ArticleBiophysical journal2002
Solid-state 19F-NMR analysis of 19F-labeled tryptophan in gramicidin A in oriented membranes.
Article in Biophysical journal, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 57 citations in OpenAlex.
- Side Chain Structures of the Proton-Selective Histidine and Gating Tryptophan in Influenza BM2 Reveal Both Conservation and Variation of the Proton Conduction Mechanism.Biochemistry · 2025Article
- The Conformational Equilibria of a Human GPCR Compared between Lipid Vesicles and Aqueous Solutions by IntegrativeJournal of the American Chemical Society · 2025Article
- Origin of the multi-phasic quenching dynamics in the BLUF domains across the species.Nature communications · 2024Article
- Determination of accurateJournal of magnetic resonance (San Diego, Calif. : 1997) · 2022Article
- Orientation and Location of the Cyclotide Kalata B1 in Lipid Bilayers Revealed by Solid-State NMR.Biophysical journal · 2017Article
- Structural and dynamic basis of phospholamban and sarcolipin inhibition of Ca(2+)-ATPase.Biochemistry · 2008Review
- Solid-state NMR analysis of the PGLa peptide orientation in DMPC bilayers: structural fidelity of 2H-labels versus high sensitivity of 19F-NMR.Biophysical journal · 2006Article
- Effects of Phe-to-Trp mutation and fluorotryptophan incorporation on the solution structure of cardiac troponin C, and analysis of its suitability as a potential probe for in situ NMR studies.Protein science : a publication of the Protein Society · 2005Article
- Structure determination of membrane proteins by NMR spectroscopy.Chemical reviews · 2004Review
- Structure of (KIAGKIA)3 aggregates in phospholipid bilayers by solid-state NMR.Biophysical journal · 2004Article
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The response of membrane-associated peptides toward the lipid environment or other binding partners can be monitored by solid-state NMR of suitably labeled side chains. Tryptophan is a prominent amino acid in transmembrane helices, and its (19)F-labeled analogues are generally biocompatible and cause little structural perturbation. Hence, we use 5F-Trp as a highly sensitive NMR probe to monitor the conformation and dynamics of the indole ring. To establish this (19)F-NMR strategy, gramicidin A was labeled with 5F-Trp in position 13 or 15, whose chi(1)/chi(2) torsion angles are known from previous (2)H-NMR studies. First, the alignment of the (19)F chemical shift anisotropy tensor within the membrane was deduced by lineshape analysis of oriented samples. Next, the three principal axes of the (19)F chemical shift anisotropy tensor were assigned within the molecular frame of the indole ring. Finally, determination of chi(1)/chi(2) for 5F-Trp in the lipid gel phase showed that the side chain alignment differs by up to 20 degrees from its known conformation in the liquid crystalline state. The sensitivity gain of (19)F-NMR and the reduction in the amount of material was at least 10-fold compared with previous (2)H-NMR studies on the same system and 100-fold compared with (15)N-NMR.
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