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Computer simulations of the properties of the α2, α2C, and α2D de novo designed helical proteins

✍ Scribed by Andrzej Sikorski; Andrzej Kolinski; Jeffrey Skolnick

Publisher
John Wiley and Sons
Year
2000
Tongue
English
Weight
286 KB
Volume
38
Category
Article
ISSN
0887-3585

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✦ Synopsis

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 studied. The energies of various topologies are similar, especially for the ␣ 2 polypeptide. The simulated crossover from molten globule to nativelike behavior is very similar to that seen in experimental studies. Simulations on a reduced protein model reproduce most of the experimental properties of the ␣ 2 , ␣ 2 C, and ␣ 2 D proteins. Stable four-helix bundle structures were obtained, with increasing native-like behavior on-going from ␣ 2 to ␣ 2 D that mimics experiment. Proteins 2000;38:17-28.

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