Large macromolecular machines, such as proteins and their complexes, are typically very flexible at physiological conditions. Computationally, this flexibility can be approximated with just a few collective molecular motions, computed e.g. using the Normal Mode Analysis (NMA). NMA determines low-frequency motions at a very low cost and these are particularly interesting to the structural...
The biological function of proteins is often related to large-scale domain motions, which are induced or suppressed by the binding of a substrate or due to cosolvents. Domain motions can be related to soft hinges, flexible linker regions or -as in the case of intrinsic unfolded proteins- be native to the unfolded protein structure. These large-scale domain motions in solution cannot be...
Protein-protein interactions can influence a range of material properties and dynamic/kinetic behaviors, from aggregation kinetics to solution viscosity, self-association, and solubility. This presentation focuses on dilute and concentrated solutions of monoclonal antibodies and synthetic antibodies, from the perspective of predicting the physical properties and/or behavior of these systems...
Approximately 10-40% of the intra- and extracellular fluids of living organisms is occupied by macromolecules such as proteins, the internal dynamics of which is widely recognized as a crucial aspect for their function. The rather high concentration of such macromolecules is known as “macromolecular crowding” and was shown to influence reaction rates [1] and protein thermal stability. Here, we...
Concentrated solutions of monoclonal antibodies have attracted considerable attention due to their importance in pharmaceutical formulations, yet their tendency to aggregate and the resulting high solution viscosity has posed considerable problems. It remains a very difficult task to understand and predict the solution behavior and stability of such solutions.
In this talk I will discuss a...
