Moerz, Sebastian T.Sebastian T.MoerzHuber, PatrickPatrickHuber2021-04-192021-04-192014-03-18Langmuir 30 (10): 2729-2737 (2014-03-18)http://hdl.handle.net/11420/9328Bovine heart cytochrome c has been immobilized into the mesoporous silica host material SBA-15 in both its native folded and urea-unfolded state. The comparison of the two folding states' behavior casts doubt on the commonly used explanation of cytochrome c adsorption, i.e. the electrostatic interaction model. A detailed investigation of the protein binding as a function of pH and ionic strength of the buffer solution reveals the complex nature of the protein-silica interaction. Electrostatic interaction, van der Waals forces and entropic contributions by counterion release each contribute to adsorption on the silica pore walls.en0743-746320141027292737Physics - Biological PhysicsPhysics - Biological PhysicsPhysics - Mesoscopic Systems and Quantum Hall EffectPhysics - Materials SciencePhysics - Soft Condensed MatterPhysics - Chemical PhysicsJournal Article10.1021/la404947j245712631503.02704v1Other