title: Folding models of mini-protein FSD-1.
abstract: We have carried out all-atom action-derived molecular dynamics (ADMD) folding simulations of the full-size FSD-1. FSD-1 is a designed mini-protein of 28 residues containing both α and β secondary structure elements. Multiple folding pathways are found for FSD-1, which is consistent with existing computational studies. Hydrophobic collapse is observed first, and then subsequent folding events proceeds by forming either α-helix or β-hairpin. Concurrent formation of the full tertiary structure and the secondary structure elements of α-helix and β-hairpin is observed. The folding pathway of FSD-1 elucidated by ADMD simulations does not follow the scenario of the framework model. ADMD simulations provide significant insights for the general mechanisms of protein folding and conformational changes.
authors.affiliation: Korea Research Institute of Standards and Science, Daejeon 305-340, Korea.
authors.forename: In-Ho
authors.initials: IH
authors.lastname: Lee
authors.forename: Seung-Yeon
authors.initials: SY
authors.lastname: Kim
authors.forename: Jooyoung
authors.initials: J
authors.lastname: Lee
mesh_terms: D004268:DNA-Binding Proteins / Q000737:chemistry*; D008958:Models, Molecular; D056004:Molecular Dynamics Simulation; D017510:Protein Folding; D017433:Protein Structure, Secondary; D014157:Transcription Factors / Q000737:chemistry*
chemical_list: D004268:DNA-Binding Proteins; C108466:FSD-1 protein, synthetic; D014157:Transcription Factors