The　influence　of　the　protein　topology-encoded　dynamical　properties　on　its　thermal　unfolding　motions　was　studied　in　the　present　work.　The　intrinsic　dynamics　of　protein　topology　was　obtained　by　the　anisotropic　network　model　(ANM).　The　ANM　has　been　largely　used　to　investigate　protein　collective　functional　motions,　but　it　is　not　well　elucidated　if　this　model　can　also　reveal　the　preferred　large-scale　motions　during　protein　unfolding.　A　small　protein　barnase　is　used　as　a　typical　case　study　to　explore　the　relationship　between　protein　topology-encoded　dynamics　and　its　unfolding　motions.　Three　thermal　unfolding　simulations　at　500　K　were　performed　for　barnase　and　the　entire　unfolding　trajectories　were　sampled　and　partitioned　into　several　windows.　For　each　window,　the　preferred　unfolding　motions　were　investigated　by　essential　dynamics　analysis,　and　then　associated　with　the　intrinsic　dynamical　properties　of　the　starting　conformation　in　this　window,　which　is　detected　by　ANM.　The　results　show　that　only　a　few　slow　normal　modes　imposed　by　protein　structure　are　sufficient　to　give　a　significant　overlap　with　the　preferred　unfolding　motions.　Especially,　the　large　amplitude　unfolding　movements,　which　imply　that　the　protein　jumps　out　of　a　local　energy　basin,　can　be　well　described　by　a　single　or　several　ANM　slow　modes.　Besides　the　global　motions,　it　is　also　found　that　the　local　residual　fluctuations　encoded　in　protein　structure　are　highly　correlated　with　those　in　the　protein　unfolding　process.　Furthermore,　we　also　investigated　the　relationship　between　protein　intrinsic　flexibility　and　its　unfolding　events.　The　results　show　that　the　intrinsic　flexible　regions　tend　to　unfold　early.　Several　early　unfolding　events　can　be　predicted　by　analysis　of　protein　structural　flexibility.　These　results　imply　that　protein　structure-encoded　dynamical　properties　have　significant　influences　on　protein　unfolding　motions.