Experimentally determined hydrophobicity scale for proteins at membrane interfaces

By William C. Wimley, S. White. 1996

The partitioning of membrane-active oligopeptides into membrane interfaces promotes the formation of secondary structure. A quantitative description of the coupling of structure formation to partitioning, which may provide a basis for understanding membrane protein folding and insertion, requires an appropriate free energy scale for partitioning. A complete interfacial hydrophobicity scale that includes the contribution of the peptide bond was therefore determined from the partitioning of two series of small model peptides into the interfaces of neutral (zwitterionic) phospholipid membranes. Aromatic residues are found to be especially favoured at the interface while charged residues, and the peptide bond, are disfavoured about equally. Reduction of the high cost of partitioning the peptide bond through hydrogen bonding may be important in the promotion of structure formation in the membrane interface.

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Citations in the corpus

Dissecting the Specificity of Protein-Protein Interaction in Bacterial Two-Component Signaling: Orphans and Crosstalks (2011, methodology): “We are grateful to R.A. White and J.A. Hoch, who were involved in early stages of this project, and to M.T. Laub for communicating unpublished results.”
Topology Prediction of α-Helical Transmembrane Proteins (2016, methodology): “• Experimental-based scales were developed by Hopp [77], Goldman [78], Wimley [79], Hessa [7] and Moon [72] and are experimentally based.”
Enhancing the stability and solubility of TEV protease using in silico design (2007, methodology): “We used, for that purpose, several amino acid polarity scales (Fauchere and Pliska 1983; Eisenberg et al. 1984; Wimley and White 1996).”
The CamSol method of rational design of protein mutants with enhanced solubility. (2015, methodology): “(1), the CamSol method uses secondary structure propensities calculated from the Protein Data Bank (PDB) using representative structures at a 50% sequence identity and a hydrophobicity scale adapted using the Wimley–White scale [57] (Table S3).”
The role of electrostatic and nonpolar interactions in the association of peripheral proteins with membranes (2002, background): “…= YifLlA, where yif is the interfacial aromatic surface tension coefficient (Yif = 0.13 kcal/mol/A1 derived from the partitioning data of Wimley and White (1996) and M is the change in solvent-accessible surface area of the aromatic side chains as the peptide associates with the…”
Melittin: a Membrane-active Peptide with Diverse Functions (2007, background): “Wimley and White (1996) have shown that the partitioning of peptides in membranes is dominated by the extremely unfavorable free energy cost of partitioning the peptide bonds (+1.2 kcal mol–1 per peptide bond for phosphocholine bilayers).”
Recognition of transmembrane helices by the endoplasmic reticulum translocon (2005, background): “and are known to interact preferentially with the headgroup region of model phospholipid bilayer”
APD: the Antimicrobial Peptide Database (2004, background): “Trp is also counted as a hydrophobic residue because of its importance in lipid binding (10,11) and preference in the protein±membrane interface (12).”
Design of a specific peptide against phenolic glycolipid-1 from Mycobacterium leprae and its implications in leprosy bacilli entry (2022, background): “(15) Another parameter was the Wimley-White whole residue hydrophobicity; more negative values for peptides indicate a higher hydrophobicity.(16) Other properties, such as the highest hydrophobic ratio percentage and the maximum number of hydrophobic residues on the same surface, were considered key”
Five computational developability guidelines for therapeutic antibody profiling (2019, background): “tested were Kyte and Doolittle (31), Wimley and White (32), Hessa et al.”