Side-chain hydrophobicity scale derived from transmembrane protein folding into lipid bilayers
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Side-chain hydrophobicity scale derived from transmembrane protein folding into lipid bilayers
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Membrane Protein Integration and Topogenesis at the ER
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Lipid bilayer regulation of membrane protein function: gramicidin channels as molecular force probes
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Tryptophan, more than just an interfacial amino acid in the membrane activity of cationic cell-penetrating and antimicrobial peptides, Quarterly Reviews of Biophysics
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Refining amino acid hydrophobicity for dynamics simulation of membrane proteins [PeerJ]
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The Hydrophobic Effect Is a Principal Force Stabilizing Tertiary and Quaternary Structures - LabXchange
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How bilayer properties influence membrane protein folding - Corin - 2020 - Protein Science - Wiley Online Library
Structural Biochemistry/Chemical Bonding/Hydrophobic interaction/Hydrophobicity scales - Wikibooks, open books for an open world
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Frontiers 3D interaction homology: The hydrophobic residues alanine, isoleucine, leucine, proline and valine play different structural roles in soluble and membrane proteins
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Membrane-mediated protein interactions drive membrane protein organization
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Transmembrane protein - Wikipedia
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Chapter 2: Protein Structure - Chemistry
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Dawn of a New Era for Membrane Protein Design