Understanding Key Elements of Protein Folding
Medical, Health Informatics and Computational Biology Accomplishment | 2005
Where the work was done: IBM T.J. Watson Research Center
What we accomplished: The 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:
- Science 2004: “Hydrophobic Collapse in Multidomain Protein Folding” (376 citations, 2/15/2016)
- Nature 2005: “Observation of a Dewetting Transition in the Collapse of the Melittin Tetramer” (273 citations, 2/15/2016)
Image credit: IBM Research Blog