De novo structure prediction and experimental characterization of folded peptoid oligomers
β Scribed by Butterfoss, G. L.; Yoo, B.; Jaworski, J. N.; Chorny, I.; Dill, K. A.; Zuckermann, R. N.; Bonneau, R.; Kirshenbaum, K.; Voelz, V. A.
- Book ID
- 115440719
- Publisher
- National Academy of Sciences
- Year
- 2012
- Tongue
- English
- Weight
- 728 KB
- Volume
- 109
- Category
- Article
- ISSN
- 0027-8424
No coin nor oath required. For personal study only.
π SIMILAR VOLUMES
## Abstract Routine structure prediction of new folds is still a challenging task for computational biology. The challenge is not only in the proper determination of overall fold but also in building models of acceptable resolution, useful for modeling the drug interactions and proteinβprotein comp
Coiled coils possess a quaternary structure comprised of the side-by-side arrangement of β£-helices. Due their inherent structural simplicity, they are ideal model systems for both theoretical and experimental studies. Among the coiled coils are the leucine zippers, which play an important role in th