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
β¦ LIBER β¦
Computer Simulations of De Novo Designed Helical Proteins
β Scribed by Sikorski, Andrzej; Kolinski, Andrzej; Skolnick, Jeffrey
- Book ID
- 119411360
- Publisher
- Biophysical Society
- Year
- 1998
- Tongue
- English
- Weight
- 271 KB
- Volume
- 75
- Category
- Article
- ISSN
- 0006-3495
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## Abstract We have designed a series of 15 short, helical de novo peptides consisting of lysine, isoleucine, and alanine. We have termed this the KIA series. These peptides differ only in their hydrophobic interface, and thus their selfβassociation is largely a consequence of hydrophobic interacti