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Designer Proteins: On the Art of Synthesizing De Novo Metalloproteins

✍ Scribed by Dr. Heinz-Bernhard Kraatz


Publisher
John Wiley and Sons
Year
1994
Tongue
English
Weight
207 KB
Volume
33
Category
Article
ISSN
0044-8249

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πŸ“œ SIMILAR VOLUMES


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## Abstract We investigated the hydrophobic packing of two previously designed caviteins, LG2 and LG3, which differ by one Gly in the linker regions between the peptide sequence and the cavitand scaffold. We sought to diminish the putative native‐like properties of LG2 and LG3, and see if we could

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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

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## Abstract The pressure‐induced structural changes of a de novo designed four‐helix bundle protein, (α‐l‐α)~2~, in aqueous solution have been investigated by FTIR spectroscopy. Changes in the amide I' band intensity show that pressure induces disruption of tertiary interactions and stabilizes the