Reduced lattice models of the three de novo designed helical proteins β£ 2 , β£ 2 C, and β£ 2 D were studied. Low temperature stable folds were obtained for all three proteins. In all cases, the lowest energy folds were four-helix bundles. The folding pathway is qualitatively the same for all proteins
Computational de novo Design, and Characterization of an A2B2 Diiron Protein
β Scribed by Christopher M Summa; Michael M Rosenblatt; Jae-Kyoung Hong; James D Lear; William F DeGrado
- Book ID
- 117142912
- Publisher
- Elsevier Science
- Year
- 2002
- Tongue
- English
- Weight
- 843 KB
- Volume
- 321
- Category
- Article
- ISSN
- 0022-2836
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## Abstract Quinones and quinoproteins are essential redox components and enzymes in biological systems. Here, we report the de novo design, synthesis, and properties of model fourβΞ±βhelix bundle quinoproteins. The proteins were designed and constructed from three different helices with 21 or 22 am