Conformational and Stability Studies of Proteins

For this type of studies, diversified instrumental solutions may be proposed, based on both FTIR microscopy and FTIR spectroscopy.

For ultra-sensitive infrared absorption spectroscopy of biomolecules, plasmonic internal reflection microscopy will exploit the Hyperion 3000 Vis-IR microscope mounting a single point Mid-band MCT detector (10,000-600 cm-1) and coupled with INVENIO-R Fourier Transform Infrared Spectrometer (Bruker). More conventional studies on deuterated proteins and dehydrated thin layers exploits INVENIO-R interferometers and dedicated accessories: liquid cells and Attenuated Total Reflection accessories (both multiple and single reflection).

Exploration of protein folding, aggregation self-assembly, and the effects of pH on protein structure with UV Resonance Raman spectroscopy takes advantage of the sensitivity and molecular selectivity of this vibrational technique. For this type of studies, the modifications of the system can be monitored in “real time” and in situ, with a minimum handling of the sample, using the DUV portable Resonance Raman system (Photon Systems) quipped with excitation wavelength at 248 nm.
Different solutions for the sampling (in bulk, using a micro-probe with micrometric resolution, in a flow cell to avoid photodegradation) are available in the lab, as well as the possibility to investigate the samples in a wide temperature range between -190 and 600 °C. Additionally, the tunable UV Resonance Raman micro-setup (Crisel Instrument) will allow to study the protein systems by varying the excitation wavelength in the range 210-270 nm in order to selective enhance specific chromophoric portions of the molecules (amide linkages, aromatic aminoacids side chains). Two sampling modalities, macro- and micro-sampling with lateral resolution of few µm, are available to achieve the specific user’s experimental requirements.