Protein folding studies
![Protein folding of α/β -fold protein UMP-Kinase - off pathway intermediates influence folding kinetics](/17862/original-1309084291.jpg?t=eyJ3aWR0aCI6MjQ2LCJvYmpfaWQiOjE3ODYyfQ%3D%3D--8f90f4befd46d22ede9e6928b4bd270d9de2df39)
Protein folding of α/β -fold protein UMP-Kinase - off pathway intermediates influence folding kinetics
© Jochen Reinstein
Model substrate proteins that are used for chaperone-assisted folding studies are usually not well defined: the analyses are of a rather descriptive/qualitative nature. We would like to link the well- defined chaperone cycles with folding studies in which the particular folding kinetics of a substrate protein are also well understood. In a first step towards this goal, we are studying the folding of a model substrate protein, namely UMP/CMP-Kinase from Dictyostelium discoideum (UmpKdicty) with transient kinetic techniques (Stopped-Flow, quenched-flow, pressure- jump, T-Jump). In addition we apply and continously develop software and instruments for rapid kinetic techniques and data acquisition.