20 DVL                   Douglas V. Laurents

Senior Scientist (since Dec. 2017)


WoS Reseacher ID: E-7527-2015 ORCID: 0000-0002-4187-165X Google Scholar:  https://scholar.google.es/citations?view_op=search_authors&mauthors=douglas+v.+Laurents+&hl=es&oi=ao

  @research line 1 @research line 2

DVL studied in protein folding and stability at Texas A&M and Stanford Universities and joined the MRL in 1997 to learn to apply NMR to characterize proteins.  Some proteins do not adopt a well defined fold. These intrinsically disordered proteins or 'IDPs' play essential roles in coordinating a myriad of cell processes, but can reek havoc when they misfold to amyloid conformers.  Harmful amyloid states are implicated in over 20 neurodegenerative diseases, for example, the protein TDP-43 forms harmful amyloids implicated in ALS. Paradoxically, the protein CPEB3 forms functional amyloids that are essential to memory conaolidation and learning.  Studies are underway to uncover why TDP-43 amyloids are harmful but CPEB3 amyloids are not.

   Many 'disordered' proteins are rich in glycine and our recent works suggests they may actually adopt folded polyproline II helices.  Our ongoing research will test this hypothesis and provide the bases so that polyproline II helices can be designed with useful functions and higher ordered structures for Biotechnology.
  • IP of three consecutive projects from the Spanish State Research Plan since 2010; a fourth project is currently under evaluation.