title: Minimal folding pathways for coarse-grained biopolymer fragments.
abstract: The minimal folding pathway or trajectory for a biopolymer can be defined as the transformation that minimizes the total distance traveled between a folded and an unfolded structure. This involves generalizing the usual Euclidean distance from points to one-dimensional objects such as a polymer. We apply this distance here to find minimal folding pathways for several candidate protein fragments, including the helix, the beta-hairpin, and a nonplanar structure where chain noncrossing is important. Comparing the distances traveled with root mean-squared distance and mean root-squared distance, we show that chain noncrossing can have large effects on the kinetic proximity of apparently similar conformations. Structures that are aligned to the beta-hairpin by minimizing mean root-squared distance, a quantity that closely approximates the true distance for long chains, show globally different orientation than structures aligned by minimizing root mean-squared distance.
authors.affiliation: Department of Physics and Astronomy, University of British Columbia, Vancouver, British Columbia, Canada.
authors.forename: Ali R
authors.initials: AR
authors.lastname: Mohazab
authors.forename: Steven S
authors.initials: SS
authors.lastname: Plotkin
mesh_terms: D001221:Aspartate Carbamoyltransferase / Q000737:chemistry / Q000378:metabolism; D001704:Biopolymers / Q000737:chemistry / Q000378:metabolism; D008958:Models, Molecular; D010446:Peptide Fragments / Q000737:chemistry* / Q000378:metabolism*; D017510:Protein Folding; D017433:Protein Structure, Secondary
chemical_list: D001704:Biopolymers; D010446:Peptide Fragments; D001221:Aspartate Carbamoyltransferase