Hierarchical dynamics in allostery following ATP hydrolysis monitored by single molecule FRET measurements and MD simulations
Steffen Wolf, Benedikt Sohmen, Björn Hellenkamp, Johann Thurn, Gerhard Stock, Thorsten Hugel
Abstract
the large M-domain α-helix to the whole protein. The resulting structural asymmetry in Hsp90 leads to the collapse of a central folding substrate binding site, causing the formation of a novel collapsed state (closed state B) that we characterise structurally. We presume that similar hierarchical mechanisms are fundamental for information transfer induced by ATP hydrolysis through many other proteins.
Topics & Concepts
Allosteric regulationATP hydrolysisFörster resonance energy transferMolecular dynamicsProtein dynamicsChemistrySingle-molecule FRETBiophysicsHsp90NanosecondProtein foldingFolding (DSP implementation)MillisecondChemical physicsFluorescenceComputational chemistryBiochemistryBiologyEnzymePhysicsHeat shock proteinATPaseLaserAstronomyQuantum mechanicsOpticsElectrical engineeringEngineeringGeneHeat shock proteins researchProtein Structure and DynamicsEnzyme Structure and Function