ArticleBiophysical journal2006
Conformation and environment of channel-forming peptides: a simulation study.
Article in Biophysical journal, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
What it found
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Who cites it
10 citing papers in PubMed, 18 citations in OpenAlex.
- Peptidomics-guided 3D structural-mechanistic investigation of bovine colostrum peptides reveals multi-targetedFood chemistry: X · 2026Article
- The impact of interchain hydrogen bonding on β-hairpin stability is readily predicted by molecular dynamics simulation.Biopolymers · 2015Article
- Cholesterol lowering drug may influence cellular immune response by altering MHC II function.Journal of lipid research · 2013Article
- NMR structure of the transmembrane domain of the n-acetylcholine receptor beta2 subunit.Biochimica et biophysica acta · 2010Article
- Structural characterization of two pore-forming peptides: consequences of introducing a C-terminal tryptophan.Proteins · 2010Article
- Structure of chemokine-derived antimicrobial Peptide interleukin-8alpha and interaction with detergent micelles and oriented lipid bilayers.Biochemistry · 2009Article
- Immunity to a self-derived, channel-forming peptide in the respiratory tract.Clinical and vaccine immunology : CVI · 2008Article
- Cytoplasmic domain of human myelin protein zero likely folded as beta-structure in compact myelin.Biophysical journal · 2007Article
- Quantum Calculations On Hydrogen Bonds In Certain Water Clusters Show Cooperative Effects.Journal of chemical theory and computation · 2007Article
- Amino-acid solvation structure in transmembrane helices from molecular dynamics simulations.Biophysical journal · 2006Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
Abstract
Ion channel-forming peptides enable us to study the conformational dynamics of a transmembrane helix as a function of sequence and environment. Molecular dynamics simulations are used to study the conformation and dynamics of three 22-residue peptides derived from the second transmembrane domain of the glycine receptor (NK4-M2GlyR-p22). Simulations are performed on the peptide in four different environments: trifluoroethanol/water; SDS micelles; DPC micelles; and a DMPC bilayer. A hierarchy of alpha-helix stabilization between the different environments is observed such that TFE/water < micelles < bilayers. Local clustering of trifluoroethanol molecules around the peptide appears to help stabilize an alpha-helical conformation. Single (S22W) and double (S22W,T19R) substitutions at the C-terminus of NK4-M2GlyR-p22 help to stabilize a helical conformation in the micelle and bilayer environments. This correlates with the ability of the W22 and R19 side chains to form H-bonds with the headgroups of lipid or detergent molecules. This study provides a first atomic resolution comparison of the structure and dynamics of NK4-M2GlyR-p22 peptides in membrane and membrane-mimetic environments, paralleling NMR and functional studies of these peptides.
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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.