title: Improvement of turn structure prediction by molecular dynamics: a case study of alpha 1-purothionin.
abstract: Because of the problems in predicting a correct conformation for loop regions in homology-based prediction, disagreements are often found between the predicted models and the refined X-ray structures of the same protein in loop regions. Such a situation has been encountered for alpha 1-purothionin (alpha 1-PT). Hence, attempts have been made to improve the predicted model of alpha 1-PT by limited molecular dynamics using both AMBER and XPLOR. With molecular dynamics, the previously predicted incorrect turn region reverts to the correct conformation as seen in the X-ray refined structure. In contrast to the model which is not subjected to molecular dynamics, the improved model refines with the X-ray data of alpha 1-PT in fewer cycles, without any manual rebuilding and with comparable or better refinement statistics. Also, the improved model serves as a better starting model in the determination of the structure with the molecular replacement methods.
authors.affiliation: Department of Chemistry, Boston College, Chestnut Hill, MA 02167.
authors.forename: U
authors.initials: U
authors.lastname: Rao
authors.forename: M M
authors.initials: MM
authors.lastname: Teeter
mesh_terms: D023181:Antimicrobial Cationic Peptides; D003198:Computer Simulation; D008958:Models, Molecular; D010940:Plant Proteins / Q000737:chemistry*; D017510:Protein Folding; D017433:Protein Structure, Secondary; D012984:Software; D013997:Time Factors
chemical_list: D023181:Antimicrobial Cationic Peptides; D010940:Plant Proteins; C063948:alpha1-purothionin protein, wheat