title: Exploring the factors determining the dynamics of different protein folds.
abstract: Normal mode analyses of homologous proteins at the family and superfamily level show that slow dynamics are similar and are preserved through evolution. This study investigates how the slow dynamics of proteins is affected by variation in the protein architecture and fold. For this purpose, we have used computer-generated protein models based on idealized protein structures with varying folds. These are shown to be protein-like in their behavior, and they are used to investigate the influence of architecture and fold on the slow dynamics. We compared the dynamics of models having different folds but similar architecture and found the architecture to be the dominant factor for the slow dynamics.
authors.affiliation: Department of Informatics, University of Bergen, N-5020 Bergen, Norway.
authors.forename: S M
authors.initials: SM
authors.lastname: Hollup
authors.forename: E
authors.initials: E
authors.lastname: Fuglebakk
authors.forename: W R
authors.initials: WR
authors.lastname: Taylor
authors.forename: N
authors.initials: N
authors.lastname: Reuter
mesh_terms: D003198:Computer Simulation; D005418:Flavodoxin / Q000737:chemistry; D054477:Glutaredoxins / Q000737:chemistry; D008958:Models, Molecular; D017510:Protein Folding; D055550:Protein Stability; D017433:Protein Structure, Secondary; D011506:Proteins / Q000737:chemistry*; D018709:Statistics, Nonparametric
chemical_list: D005418:Flavodoxin; D054477:Glutaredoxins; D011506:Proteins