Proteiners struktur och funktion II

Do proteins really need chaperones to fold, how do macromolecular motors assemble and operate, and why do proteins sometimes aggregate to cause neurodegenerative disease? These questions are dealt with in this course, where equilibrium behaviour is extended to kinetics and the functional role of high-energy transition states. In this course you will learn, hands on, how to structurally characterise protein-folding transition states by protein engineering, structural determination of large complexes by cryo-EM and protein NMR. The course contains also an introduction to how cells orchestrate and maintains protein function at molecular level and outlines the current view and complexity of protein-aggregation disease. The key aim is to understand the concept of how amino-acid properties control (i) protein self-assembly and (ii) higher-order processes such as solubility, behaviour in crowded intracellular environments, and protein aggregation. The basic theme of the course is that theory, wet-labs and computing go hand-in-hand to solve real problems in protein chemistry. As such, reductionist thinking, application of basic chemical models and data quantification constitute a red thread throughout the teaching, and several common spectroscopic methods and experimental approaches are employed in depth. Experimental results, progress and student conclusions will be presented/examined both in form of individual seminars, written reports and poster presentations.