タンパク質のフォールディングシミュレーション(<小特集>「ナノ, バイオテクノロジーにおける分子動力学シミュレーション」)

概要

論文の詳細を見る
Despite the huge size of conformational space in the unfolded states, protein molecules quickly fold into a unique native structure. To study the folding process of small proteins, the molecular dynamics simulation at atomic resolution has become recently a realistic and powerful tool as well as the experimental methods. Here a computational study on the folding of mini-protein, Trp-cage, is briefly introduced. From a number of long simulations performed on the computational grid (the Titech Grid at Tokyo Institute of Technology), a lot of folding and unfolding events were captured. A phylogenetic tree of these trajectories was depicted using the "trajectory alignments", a novel analytical method for the trajectory comparison and classification. This phylogeny reveales a unique folding pathway to the native structure.
日本シミュレーション学会の論文
2005-09-15