title: Hydrogen-bond energetics drive helix formation in membrane interfaces.
abstract: The free energy cost ΔG of partitioning many unfolded peptides into membrane interfaces is unfavorable due to the cost of partitioning backbone peptide bonds. The partitioning cost is dramatically reduced if the peptide bonds participate in hydrogen bonds. The reduced cost underlies secondary structure formation by amphiphilic peptides partitioned into membrane interfaces through a process referred to as partitioning-folding coupling. This coupling is characterized by the free energy reduction per residue, ∆G(res) that drives folding. There is some debate about the correct value of ∆G(res) and its dependence on the hydrophobic moment (μ(H)) of amphiphilic α-helical peptides. We show how to compute ∆G(res) correctly. Using published data for two families of peptides with different hydrophobic moments and charges, we find that ∆G(res) does not depend upon μ(H). The best estimate of ∆G(res) is -0.37 ± 0.02 kcal mol(-1). This article is part of a Special Issue entitled: Membrane protein structure and function.
authors.affiliation: Department of Chemistry and Biochemistry, University of North Carolina Wilmington, Wilmington, NC 28403, USA.
authors.forename: Paulo F
authors.initials: PF
authors.lastname: Almeida
authors.forename: Alexey S
authors.initials: AS
authors.lastname: Ladokhin
authors.forename: Stephen H
authors.initials: SH
authors.lastname: White
mesh_terms: D006860:Hydrogen Bonding; D008565:Membrane Proteins / Q000737:chemistry*; D010455:Peptides / Q000737:chemistry; D017510:Protein Folding; D017433:Protein Structure, Secondary; D013816:Thermodynamics
chemical_list: D008565:Membrane Proteins; D010455:Peptides