ArticleBiochemistry2007
Orientation and motion of tryptophan interfacial anchors in membrane-spanning peptides.
Article in Biochemistry, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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Who cites it
31 citing papers in PubMed, 53 citations in OpenAlex.
- ToxMamba: a novel method for toxic peptide prediction based on the fusion of pretrained embeddings and multi-scale state space models.Briefings in bioinformatics · 2026Article
- LEAP2 in Physiology-A Narrative Review.International journal of molecular sciences · 2025Review
- NMR identification of a conserved Drp1 cardiolipin-binding motif essential for stress-induced mitochondrial fission.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- The Uniqueness of Tryptophan in Biology: Properties, Metabolism, Interactions and Localization in Proteins.International journal of molecular sciences · 2020Review
- Influence of interfacial tryptophan residues on an arginine-flanked transmembrane helix.Biochimica et biophysica acta. Biomembranes · 2020Article
- Breaking the Backbone: Central Arginine Residues Induce Membrane Exit and Helix Distortions within a Dynamic Membrane Peptide.The journal of physical chemistry. B · 2019Article
- Control of Transmembrane Helix Dynamics by Interfacial Tryptophan Residues.Biophysical journal · 2018Article
- New applications of solid-state NMR in structural biology.Emerging topics in life sciences · 2018Article
- Emerging complexities of lipid regulation of potassium channels.The Journal of general physiology · 2016Article
- Novel pH-Sensitive Cyclic Peptides.Scientific reports · 2016Article
- A Conserved Residue Cluster That Governs Kinetics of ATP-dependent Gating of Kir6.2 Potassium Channels.The Journal of biological chemistry · 2015Article
- Comparisons of interfacial Phe, Tyr, and Trp residues as determinants of orientation and dynamics for GWALP transmembrane peptides.Biochemistry · 2014Article
- Single tryptophan and tyrosine comparisons in the N-terminal and C-terminal interface regions of transmembrane GWALP peptides.The journal of physical chemistry. B · 2013Article
- Canonical azimuthal rotations and flanking residues constrain the orientation of transmembrane helices.Biophysical journal · 2013Article
- Properties of membrane-incorporated WALP peptides that are anchored on only one end.Biochemistry · 2012Article
- Tyrosine replacing tryptophan as an anchor in GWALP peptides.Biochemistry · 2012Article
- Isotope labeling for solution and solid-state NMR spectroscopy of membrane proteins.Advances in experimental medicine and biology · 2012Review
- Response of GWALP transmembrane peptides to changes in the tryptophan anchor positions.Biochemistry · 2011Article
- The membrane interface dictates different anchor roles for "inner pair" and "outer pair" tryptophan indole rings in gramicidin A channels.Biochemistry · 2011Article
- Tryptophan-lipid interactions in membrane protein folding probed by ultraviolet resonance Raman and fluorescence spectroscopy.Biophysical journal · 2011Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
The tryptophans of integral membrane proteins have been suggested to play specific roles as "interfacial anchors", based on their preference for a location near the lipid head groups. Still, the underlying mechanism behind this behavior remains unclear. NMR experiments can provide an important tool to study this interaction in an actual bilayer environment. Here solid-state deuterium nuclear magnetic resonance was used to study the tryptophans in membrane-spanning model peptides from the WALP family (acetyl-GWW(LA)nWWA-ethanolamide with n = 5 and 6.5) in samples of mechanically aligned dimyristoylphosphatidylcholine (DMPC) bilayers. The data indicate that the tryptophans near the C-terminal end of the peptide display a significantly different behavior from those near the N-terminus. This is reflected prominently in a large difference in the motion experienced by the indoles at either end of the peptide, highlighting the directionality of the helix. Nevertheless, our observations indicate high levels of motional freedom for all tryptophans in these membrane spanning domains that exceed the dynamics for the helix itself. These observations signify that steric and dynamic features of the polypeptide context modulate the tryptophan anchoring in the membrane interface. Measurements of WALP19 in the ether-linked DMPC analogue ditetradecylphosphatidylcholine (missing the lipid carbonyls) show very similar Trp dynamics and suggest similar orientations for some or all of the tryptophans. This suggests that the lipid acyl chain carbonyls play at most a minor role in the anchoring interaction between these Trp residues and the DMPC interfacial region.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.