title: Computational investigations of folded self-avoiding walks related to protein folding.
abstract: Various subsets of self-avoiding walks naturally appear when investigating existing methods designed to predict the 3D conformation of a protein of interest. Two such subsets, namely the folded and the unfoldable self-avoiding walks, are studied computationally in this article. We show that these two sets are equal and correspond to the whole n-step self-avoiding walks for n≤14, but that they are different for numerous n≥108, which are common protein lengths. Concrete counterexamples are provided and the computational methods used to discover them are completely detailed. A tool for studying these subsets of walks related to both pivot moves and protein conformations is finally presented.
authors.affiliation: FEMTO-ST Institute, UMR 6174 CNRS, University of Franche-Comté, Besançon, France. Electronic address: jacques.bahi@femto-st.fr.
authors.forename: Jacques M
authors.initials: JM
authors.lastname: Bahi
authors.forename: Christophe
authors.initials: C
authors.lastname: Guyeux
authors.forename: Kamel
authors.initials: K
authors.lastname: Mazouzi
authors.forename: Laurent
authors.initials: L
authors.lastname: Philippe
mesh_terms: D000465:Algorithms; D003198:Computer Simulation; D017510:Protein Folding; D011506:Proteins / Q000737:chemistry*; D012984:Software
chemical_list: D011506:Proteins
keywords: Protein folding; Protein structure prediction; Self avoiding walks