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Dissection of the de Novo Designed Peptide αtα: Stability and Properties of the Intact Molecule and Its Constituent Helices †

✍ Scribed by Fezoui, Youcef; Braswell, Emory H.; Xian, Wujing; Osterhout, John J.


Book ID
126184496
Publisher
American Chemical Society
Year
1999
Tongue
English
Weight
143 KB
Volume
38
Category
Article
ISSN
0006-2960

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Reduced lattice models of the three de novo designed helical proteins ␣ 2 , ␣ 2 C, and ␣ 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