Side-chain hydrophobicity scale derived from transmembrane protein folding into lipid bilayers
Price: $ 33.99
4.8(458)
Lipid bilayer induces contraction of the denatured state ensemble of a helical-bundle membrane protein
Systematic Design and Validation of Ion Channel Stabilization of Amphipathic α-Helical Peptides Incorporating Tryptophan Residues
Energetics of side-chain partitioning of β-signal residues in unassisted folding of a transmembrane β-barrel protein - ScienceDirect
Chapter 6 - Cell and Organelle Membrane Structure” in “Fundamentals of Cell Biology”
Hydrophobicity scales - Wikipedia
Structure
Role of the lipid bilayer in outer membrane protein folding in Gram-negative bacteria - ScienceDirect
The energetics of transmembrane helix insertion and the consequences
Figure 5 from Curvature Forces in Membrane Lipid − Protein Interactions
Curvature Forces in Membrane Lipid–Protein Interactions
Frontiers Comparison of hydrophobicity scales for predicting biophysical properties of antibodies
