1-2-dilauroylphosphatidylcholine has been researched along with dodecylphosphocholine* in 1 studies
1 other study(ies) available for 1-2-dilauroylphosphatidylcholine and dodecylphosphocholine
| Article | Year |
|---|---|
Energetics of side-chain partitioning of β-signal residues in unassisted folding of a transmembrane β-barrel protein.
The free energy of water-to-interface amino acid partitioning is a major contributing factor in membrane protein folding and stability. The interface residues at the C terminus of transmembrane β-barrels form the β-signal motif required for assisted β-barrel assembly Topics: Acyltransferases; Amino Acid Motifs; Amino Acids; Energy Transfer; Enzyme Stability; Escherichia coli K12; Escherichia coli Proteins; Gene Deletion; Hydrophobic and Hydrophilic Interactions; Lipid Bilayers; Micelles; Models, Molecular; Molecular Dynamics Simulation; Phosphatidylcholines; Phosphorylcholine; Protein Conformation, beta-Strand; Protein Folding; Protein Interaction Domains and Motifs; Protein Structure, Secondary; Surface Properties; Thermodynamics | 2017 |