Lattice model of transmembrane polypeptide folding
- 18 December 2000
- journal article
- research article
- Published by American Physical Society (APS) in Physical Review E
- Vol. 63 (1) , 010901
- https://doi.org/10.1103/physreve.63.010901
Abstract
Folding of hydrophobic polypeptides into unique three-dimensional structures in a membrane is investigated by Monte Carlo simulations using the bond fluctuation model. Its ground state structure can be a helix or a double helix depending on the competition of hydrogen bonding and backbone bending energies. The folding pathway of hydrophobic polypeptides in a nonpolar environment is found to favor the helical structure over the double helix. The folding time of a transmembrane domain increases exponentially with the chain length. Folding at low temperatures exhibits an Arrhenius-like behavior. We discuss the kinetics of both random folding and channel complex assisted folding of a polypeptide chain. Our results suggest a significantly smaller energetic barrier in the folding pathway for channel complex assisted folding.Keywords
This publication has 24 references indexed in Scilit:
- MEMBRANE PROTEIN FOLDING AND STABILITY: Physical PrinciplesAnnual Review of Biophysics, 1999
- THEORY OF PROTEIN FOLDING: The Energy Landscape PerspectiveAnnual Review of Physical Chemistry, 1997
- SOLVATION: HOW TO OBTAIN MICROSCOPIC ENERGIES FROM PARTITIONING AND SOLVATION EXPERIMENTSAnnual Review of Biophysics, 1997
- Chain Length Scaling of Protein Folding TimePhysical Review Letters, 1996
- Emergence of Preferred Structures in a Simple Model of Protein FoldingScience, 1996
- Navigating the Folding RoutesScience, 1995
- Spontaneous insertion of polypeptide chains into membranes: a Monte Carlo model.Proceedings of the National Academy of Sciences, 1992
- Protein folding funnels: a kinetic approach to the sequence-structure relationship.Proceedings of the National Academy of Sciences, 1992
- Membrane protein folding and oligomerization: the two-stage modelBiochemistry, 1990
- Intermediates and barrier crossing in a random energy model (with applications to protein folding)The Journal of Physical Chemistry, 1989