Single-molecule vectorial protein folding and unfolding

 

Seminar

Single-molecule vectorial protein folding and unfolding

David Rodriguez- Larrea, PhD

Single-molecule vectorial protein folding and unfolding Protein folding and unfolding is inherently linked to protein homeostasis. When proteins are synthesized they usually acquire a 3D structure (folding) that allows a given function. Protein unfolding, on the other hand, is required for proteasomal degradation and for many transport phenomena across membranes. Our current knowledge suggest that in these cases protein folding and unfolding is vectorial (it starts at one end of the polypeptide chain and moves towards the other end). Here I will show how nanopore technology allows observation of vectorial folding and unfolding on single-molecules. Furthermore, this technology can determine the phosphorylation pattern on single protein molecules and to quantify each of the possible species. Eventually, these approaches can lead to single-molecule protein sequencing and to a deeper understanding of protein homeostasis. Dr. Rodríguez-Larrea obtained his PhD degree at the Universidad de Granada studying protein stability under the supervision of JM Sánchez-Ruiz, and worked as postdoctoral researcher with H Bailey at the University of Oxford using single-molecule methods to study protein folding. He has recently joined the Unidad de Biofísica, Leioa, as a Ramón y Cajal Researcher and Principal Investigator.