Understanding Key Elements of Protein Folding       

Medical, Health Informatics and Computational Biology Accomplishment | 2005

IBM researchers: Ruhong Zhou, Bruce Berne

Where the work was done: IBM T.J. Watson Research Center

What we accomplishedThe team used computer simulation to understand the key events that cause proteins to fold

  • Paraphrasing Wikipedia, protein folding is the "process by which a protein chain acquires its native 3-dimensional structure in an expeditious and reproducible manner.  This 3-dimensional structure is usually biologically functional."
  • The protein folding problem is understanding the sequence of small steps which lead to proteins folding into the 3-dimensional structure used in cells, and thus underpin much of what happens in biology of larger structures above the molecular level. 
  • Hydrophobic collapse is "one of the main events necessary for proteins to reach a stable and functional state when folding."
  • Since hydrophobic collapse plays a major role in driving the folding process, understanding its nature is an important step towards understanding how and why proteins fold.
  • Using computer simulations, the IBM team investigated the dewetting transition, i.e. "rupture of a thin liquid film on a liquid or solid substrate and the formation of droplets," and found that this transition could occur when proteins fold or form large multi-protein complexes.  
  • The team also identified what physical interactions govern the dewetting critical distance as well as the collapse speed.
  • These new insights not only help in the design of better novel water nanopores and nanoscale molecular switches, but also provide deeper understanding of the mechanism behind all subcellular self-assemblies.

Related links: Key research results:

Image credit: IBM Research Blog