Dynamics in Thermotoga neapolitana adenylate kinase: [super 15]N relaxation and hydrogen-deuterium exchange studies of a hyperthermophilic enzyme highly active at 30 degree Celsius

Combination of [super 15]N NMR relaxation measurements and NMR monitored hydrogen-deuterium exchange at 30 degree Celsius was used to study the backbone conformational dynamics of Thermotoga neapolitana adenylate kinase in the free form (TNAK) and inhibitor-bound form (TNAK*Ap5A). The results revealed that TNAK maintained high activity at 30 degree Celsius by localizing flexibility to the hinge regions that are key to facilitating conformational changes.