Folding of bundles of alpha-helices in solution, membranes, and adsorbed overlayers.
We propose a coarse-grained lattice model for Monte Carlo simulations of folding of proteins consisting of several alpha-helices. A chain representing a protein is considered to contain A and B monomers forming relatively stiff A subchains, mimicking helices, and flexible B links between these subchains, respectively. Using this model, we simulate (1) folding of four-helix proteins in solution; (2) folding of membrane proteins containing one, two, or four helices; and (3) refolding of four-helix proteins adsorbed at the liquid-solid interface. For these cases, we show typical scenarios of protein folding and refolding and study the dependence of the folding time on the chain length. Combining the latter results with those already available in the literature, we discuss the relative rates of folding of proteins belonging to different classes.
Zhdanov
V P
VP
Department of Applied Physics, Chalmers University of Technology, Göteborg, Sweden. zhdanov@catalysis.nsk.su
Kasemo
B
B
D000465:Algorithms; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D003573:Cytochrome b Group / Q000737:chemistry*; D029968:Escherichia coli Proteins; D008565:Membrane Proteins / Q000737:chemistry*; D008958:Models, Molecular; D015394:Molecular Structure; D009010:Monte Carlo Method; D017510:Protein Folding; D017433:Protein Structure, Secondary; D012996:Solutions
D003573:Cytochrome b Group; D029968:Escherichia coli Proteins; D008565:Membrane Proteins; D012996:Solutions; C017850:cytochrome b562, E coli