Department home Homepage Institute Disclaimer Site Map Research Projects Gallery Publications Staff Jobs PhD programs Teaching & Conferences Downloads Contact Protein Unfolding - Polymer Physics     / home / Research Projects / Protein Unfolding - Polymer Physics / Aqueous urea solution: structure, energetics, and urea aggregation In virtually every biochemistry lab, urea is used as protein denaturant. However, despite its ubiquiteous use, only little is known about the molecular mechanism underlying urea-induced protein denaturation. To study structure and energetics of aqueous urea solutions, ... [more] Urea Driven Protein Denaturation of the Cold Shock Protein Some proteins such as the Cold Shock protein Bc-CsP are not strongly affected by the presence of urea in molecular dynamics simulations within reachable simulation times. To tackle this problem and study urea-induced unfolding for the Cold Shock protein, we generate ... [more] Ubiquitin Unfolding and Refolding Proteins enable living organisms to move, metabolize and sense, in short, to function. To fulfill such diverse tasks, proteins take up a specific fold, their native structure. The factors driving the complex folding process are not yet fully understood. Conventional ... [more] Light Driven Polymer Switching Nanomechanical devices or molecular machines will, for a broad range of applications, most likely be powered by light or other kinds of electromagnetic radiation. The major reasons are ease of addressability, picosecond reaction times to external stimuli, and ... [more] Simulation of AFM Stretching Experiments I: Mechanical Properties of Polysaccharides Elastic properties of three biologically relevant D-glucose polymers (1-6)-glucose (dextran), (1-4)-glucose (amylose), and (1-4)-glucose (cellulose) have been studied by molecular dynamics (MD) simulations. In these simulations, the sugar polymers were stretched by an ... [more] Simulation of AFM Stretching Experiments II: Mechanical Properties of Poly-Ethylenglycol (PEG) Unfolding and elastic properties of single poly(ethylene-glycol) (PEG) polymers were studied by means of molecular dynamics (MD) simulations. The simulations were performed in close resemblance to recent single molecule force spectroscopy experiments that were carried ... [more] Tension induced titin kinase activation Activation of the titin kinase, the catalytic domain of the muscle protein titin, requires major conformational rearrangements resulting in the exposure of its phosphorylation site. It can be assumed but has not yet been shown that the requisite structural change is ... © 2012, Max Planck Institute for Biophysical Chemistry, Göttingen