Broadband Dielectric Spectroscopy
Broadband Dielectric Spectroscopy probes the electrical polarization of a sample in a broad spectral range from Millihertz to Megahertz. This polarization is governed by reorientation motions of polar moieties which enables to trace the dynamics of molecules, of side groups of macromolecules as well as of ions. Mapping the thermal activation of these so-called relaxation times can help to identify structure property relations of material performances ranging from charge transport to dynamics to mechanical stability. We will provide a hands-on experience of such investigations on a diverse set of samples to compare among the groups.
Differential Scanning Calorimetry
Differential scanning calorimetry (DSC) is a standard technique used to investigate the thermal behavior of polymers. With DSC, phase transitions of polymers and proteins can be studied and correlated to the morphology. In this lab course, the students will perform DSC measurements of a typical polymer sample to determine the crystallization and glass transition parameters. Also, we will demonstrate different calorimetric devices including fast scanning calorimetry with its typical applications.
Infrared (IR) spectroscopy is a highly versatile tool in molecular physics with multiple options for refinements, e.g. combining IR spectroscopy with Fast Scanning Calorimetry (FSC) or using grazing angle IR-reflection for interface-sensitive measurements. In this lab course, basic hands-on experiments will be provided by measuring the IR spectra of several samples. By analysing the absorption characteristics which can be understood as the “vibrational fingerprint” of a polymer, the structure of the polymeric sample can be identified. The students are invited to bring their own samples.
Nuclear Magnetic Resonance (NMR)
NMR spectroscopy in its simplest form can be conducted on low-field instruments, where one is limited to measure proton spin relaxation times without any spectral resolution. These inform about the overall mobility of the molecular species, and can be used to characterize the composition of soft-matter or polymer systems with significantly inhomogeneous dynamics, such as semicrystalline polymers or food items (e.g. solid starch vs. mobile water in bread). We will provide a hands-on experience of such investigations and encourage the students to bring their own samples.
High resolution NMR on proteins
High resolution NMR spectroscopy allows studies of the structure and dynamics of proteins as well as their interactions with other biomacromolecules. The students will get an introduction to high field NMR spectroscopy and will record 1- and 2-dimensional NMR spectra of the protein ubiquitine. During the the hands-on analysis of protein NMR spectra, the students will assign NMR resonances of the protein to the respective nuclei.