May 22, 2014: News coverage in Berkeley Lab's Materials Sciences Division (MSD) website. MSD news

May 22, 2014: News coverage in Today at Berkeley Lab (TABL). TABL news

May 17-18, 2014: We exhibited at Maker Faire Bay Area. Download flier.

Apr 26, 2014: Talk and hands-on with students in grade 7-10 (to students from Johns Hopkins Center for Talented Youth).

Apr 12, 2014:
We exhibited at Lawrence Hall of Science. Featured Makers in NanoDays.

Jan, 2014:  Make Magazine article. Steps on how to make Peppytides
Promita Chakraborty and Ronald N. Zuckermann, Peppytides, MAKE Projects, Jan 2014

Sep 08, 2013: Outreach with Peppytides in the Berkeley Lab booth at the Solano Stroll 2013.


Aug 26, 2013: Work on Peppytides featured in Berkeley Science Review blog. Check out this nice post here.

Jul 29, 2013:
We have made available 
through this website, all the files and steps needed to make a Peppytide model.

Jun 25, 2013: Our first paper on Peppytides has been accepted in PNAS (

Coarse-grained, foldable, physical model of the polypeptide chain 
Promita Chakraborty and Ronald N. Zuckermann
The Molecular Foundry, Lawrence Berkeley National Laboratory, Berkeley, CA 94720
Proceedings of the National Academy of Sciences

Although nonflexible, scaled molecular models like Pauling–Corey’s and its descendants have made significant contributions in structural biology research and pedagogy, recent technical advan- ces in 3D printing and electronics make it possible to go one step further in designing physical models of biomacromolecules: to make them conformationally dynamic. We report here the design, construction, and validation of a flexible, scaled, physical model of the polypeptide chain, which accurately reproduces the bond rotational degrees of freedom in the peptide backbone. The coarse- grained backbone model consists of repeating amide and α-carbon units, connected by mechanical bonds (corresponding to φ and ψ) that include realistic barriers to rotation that closely approximate those found at the molecular scale. Longer-range hydrogen-bonding interactions are also incorporated, allowing the chain to readily fold into stable secondary structures. The model is easily constructed with readily obtainable parts and promises to be a tremendous educational aid to the intuitive understanding of chain folding as the basis for macromolecular structure. Furthermore, this physical model can serve as the basis for linking tangible bio- macromolecular models directly to the vast array of existing computational tools to provide an enhanced and interactive human– computer interface.