Another paper from the Baker lab in Science! Designed Protein Containers Push Bioengineering Boundaries.
"In this paper, former Baker lab graduate student Jacob Bale, Ph.D. and collaborators describe the computational design and experimental characterization of ten two-component protein complexes that self-assemble into nanocages with atomic-level accuracy. These nanocages are the largest designed proteins to date with molecular weights of 1.8-2.8 megadaltons and diameters comparable to small viral capsids. The structures have been confirmed by X-ray crystallography. The advantage of a multi-component protein complex is the ability to control assembly by mixing individually prepared subunits. The authors show that in vitro mixing of the designed subunits occurs rapidly and enables controlled packaging of negatively charged GFP by introducing positive charges on the interior surfaces of the two copmonents.
The ability to design, with atomic-level precision, these large protein nanostructures that can encapsulate biologically relevant cargo and that can be genetically modified with various functionalities opens up exciting new opportunities for targeted drug delivery and vaccine design." - from the IPD website.
More information can be found at this link.
Thank you all for your contributions!
We've come out with a breakthrough paper in Science titled 'De novo design
of protein homo-oligomers with modular hydrogen-bond network-mediated
This is an exciting and significant breakthrough for de novo protein
design. A particular challenge for current protein design methods has been
the accurate design of polar binding sites or polar binding interfaces,
both of which require hydrogen bonding interactions. Hydrogen bond
networks are governed by complex physics and energetic coupling, that
until now, could not be computed within the scope of design. The
computational method described in this paper, HBNet, now provides a
general method to accurately design in hydrogen bond networks. This new
capacity should be useful in the design of new enzymes, proteins that bind
small molecules, and polar protein interfaces. Thanks Rosetta@home
community for your participation and help!
The PDF of this article can be found here
article on this work was also published in Geekwire http://www.geekwire.com/2016/uw-researchers-add-new-twists-protein-designs.