Coil-helix transition of polypeptide at water-lipid interface

Abstract

We present the exact solution of a microscopic statistical mechanical model for the transformation of a long polypeptide between an unstructured coil conformation and an $\alpha$-helix conformation. The polypeptide is assumed to be adsorbed to the interface between a polar and a non-polar environment such as realized by water and the lipid bilayer of a membrane. The interfacial coil-helix transformation is the first stage in the folding process of helical membrane proteins. Depending on the values of model parameters, the conformation changes as a crossover, a discontinuous transition, or a continuous transition with helicity in the role of order parameter. Our model is constructed as a system of statistically interacting quasiparticles that are activated from the helix pseudo-vacuum. The particles represent links between adjacent residues in coil conformation that form a self-avoiding random walk in two dimensions. Explicit results are presented for helicity, entropy, heat capacity, and the average numbers and sizes of both coil and helix segments.

arXiv comment22 pages, 12 figures, accepted for publication by JSTAT

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Cited by in corpus (7)

• Coil-helix transition of polypeptide at water-lipid interface
• Molecular chains under tension: Thermal and mechanical activation of statistically interacting extension and contraction particles
• Jammed disks of two sizes and weights in a channel: Alternating sequences
• The application of the fractional exclusion statistics to the BCS theory--a redefinition of the quasiparticle energies
• Derivation of a statistical model for classical systems obeying fractional exclusion principle
• Free-energy landscapes and insertion pathways for peptides in membrane environment
• Mechanical response to tension and torque of molecular chains via statistically interacting particles associated with extension, contraction, twist, and supercoiling