Reversible transition between alpha-helix and beta-sheet conformation of a transmembrane domain.

Despite the important functions of protein transmembrane domains, their structure and dynamics are often scarcely known. The SNARE proteins VAMP/synaptobrevin and syntaxin 1 are implicated in membrane fusion. Using different spectroscopic approaches we observed a marked sensitivity of their transmembrane domain structure in regard to the lipid/peptide ratio.

Following matrix metalloproteinases activity near the cell boundary by infrared micro-spectroscopy.

Matrix Metalloproteinases (MMPs) are cell-secreted soluble and membrane-tethered enzymes that degrade extracellular matrix (ECM) proteins. These proteases play a key role in diverse physiological and pathological processes, including embryonic development, wound repair, inflammatory diseases and cancer. Yet, there is insufficient knowledge on the mode by which cell-produced MMPs conduct their action on the ECM.