title: Simulated unfolded-state ensemble and the experimental NMR structures of villin headpiece yield similar wide-angle solution X-ray scattering profiles.
abstract: With the advent of powerful synchrotron sources, solution X-ray scattering is being increasingly used to get basic information about the structure of polypeptides. The solution scattering technique essentially provides one-dimensional data, which are then interpreted in terms of a three-dimensional structure through model building. Here we calculate wide-angle solution scattering patterns for an ensemble of simulated unfolded structures of villin headpiece, which differ from the native structure by rmsd = 8.8 +/- 1.0 A and have only negligible amounts of native secondary structure. We show that the wide-angle solution scattering pattern of such an ensemble shares significant similarity with the one based on the experimental NMR structures of the molecule. Our results suggest that solution scattering in the wide-angle limit, by itself, provides very little information about the secondary structure content of a polypeptide or its side-chain packing.
authors.affiliation: Physical Chemistry Institute, ETH Zurich, 8093 Zurich, Switzerland. zagrovic@igc.phys.chem.ethz.ch
authors.forename: Bojan
authors.initials: B
authors.lastname: Zagrovic
authors.forename: Vijay S
authors.initials: VS
authors.lastname: Pande
mesh_terms: D003198:Computer Simulation; D057927:Hydrophobic and Hydrophilic Interactions; D008840:Microfilament Proteins / Q000737:chemistry*; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods; D017510:Protein Folding; D017433:Protein Structure, Secondary; D012996:Solutions; D014961:X-Ray Diffraction
chemical_list: D008840:Microfilament Proteins; D012996:Solutions; C026615:villin