Abstract: A system and method for determining the dissociation constant for a particular ligand is disclosed. In accordance with certain embodiments, the method creates a chemical denaturation curve of a protein in the absence of the ligand. A particular point is selected from this curve, such as the point at which 90% of the protein is unfolded. The molarity of chemical denaturant is determined for this selected point. A one point test is then performed for the protein with a predetermined concentration of the particular ligand. The fraction of protein which is unfolded at this point is then used to determine the dissociation constant for the ligand. This constant is used to quickly determine whether a particular ligard is well suited to be considered a potential drug candidate against that protein target.

Abstract: A system for automatically creating a denaturation curve is disclosed. In accordance with certain embodiments, a movement system including a unit having a plurality of cannulas is used. The cannulas are in fluid communication with a fluid system, which allows the cannulas to draw in and dispense fluid. A measurement system is included which draws fluid from a well into a detector to determine a characteristic of the fluid. A controller is used to control these systems and also to create a denaturation graph from the measured characteristics. In another embodiment, a plurality of formulations may be created using the system.

Abstract: A system for automatically creating a denaturation curve is disclosed. In accordance with certain embodiments, a movement system including a unit having a plurality of cannulas is used. The cannulas are in fluid communication with a fluid system, which allows the cannulas to draw in and dispense fluid. A measurement system is included which draws fluid from a well into a detector to determine a characteristic of the fluid. A controller is used to control these systems and also to create a denaturation graph from the measured characteristics. In another embodiment, a plurality of formulations may be created using the system.

Abstract: A system and method for determining the dissociation constant for a particular ligand is disclosed. In accordance with certain embodiments, the method creates a chemical denaturation curve of a protein in the absence of the ligand. A particular point is selected from this curve, such as the point at which 90% of the protein is unfolded. The molarity of chemical denaturant is determined for this selected point. A one point test is then performed for the protein with a predetermined concentration of the particular ligand. The fraction of protein which is unfolded at this point is then used to determine the dissociation constant for the ligand. This constant is used to quickly determine whether a particular ligard is well suited to be considered a potential drug candidate against that protein target.

Abstract: A system and method for creating a plurality of denaturation curves is disclosed. In accordance with certain embodiments, one variable, such as salt content, pH or another parameter, is varied to create a plurality of different buffer solutions. Each is then used to create a denaturation graph. The plurality of denaturation graphs allows analysis of the effect of that variable on protein stability.

Abstract: A system and method for creating a buffer solution having a desired pH value is disclosed. The method uses two known buffer solutions, each with predetermined pH values, and determines a mathematical relationship which defines the amount of each known buffer solution needed to create the buffer solution with the desired pH. This method can then be used to create one or more denaturation graphs, which demonstrate the stability of a protein at a given pH level.