Exploring Protein Conformational Landscapes Using High-Pressure NMR Journal Article uri icon

DCO ID 11121/9154-2730-4400-7359-CC

is Contribution to the DCO

  • YES

year of publication

  • 2018

abstract

  • Protein conformational landscapes define their functional properties as well as their proteostasis. Hence, detailed mapping of these landscapes is necessary to understand and modulate protein conformation. The combination of high pressure and NMR provides a particularly powerful approach to characterizing protein conformational transitions. First, pressure, because its effects on protein structure arise from elimination of solvent excluded void volume, represents a more subtle perturbation than chemical denaturants, favoring the population of intermediates. Second, the residue-specific and multifaceted nature of NMR observables informs on many local structural properties of proteins, aiding in the characterization of intermediate and excited states.