Ultrafast folding of α3D: A de novo designed three-helix bundle protein
By Yongjin Zhu, D. O. Alonso, K. Maki, Cheng-Yen Huang, S. Lahr, V. Daggett, H. Roder, William F. DeGrado, F. Gai. Proceedings of the National Academy of Sciences of the United States of America, 2003
143 citations recorded by the source corpus.
Subfields: General Health Professions, Occupational Therapy, Pharmacology
View Paper: https://www.semanticscholar.org/paper/1b48c20499a678bf25ca3131b8af3395abd68f16
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Citations in the corpus
- The protein folding 'speed limit'. (2004, background): “The designed three-helix bundle a3D [20] is the intrinsically fastest folding protein, with the naturally occurring three-helix bundle albumin binding domain [89] a close second (the same ranking is obtained with a weaker length dependence such as N(2)).”
- De novo protein design, a retrospective (2020, background): “…folded globular structure, α3D quickly became a very widely studied protein for computational and experimental studies of protein folding (Zhu et al., 2003; Park et al., 2006; Liu et al., 2009; Adhikari et al., 2012; Shao, 2014; Chung et al., 2015; Zeng et al., 2016; Maruyama and…”