| Autor: |
de Haas, Robbert J., Tas, Roderick P., den Broek, Daniëlle van, Chuanbao Zheng, Nguyen, Hannah, Kang, Alex, Bera, Asim K., King, Neil P., Voets, Ilja K., de Vries, Renko |
| Předmět: |
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| Zdroj: |
Proceedings of the National Academy of Sciences of the United States of America; 7/4/2023, Vol. 120 Issue 27, p1-8, 52p |
| Abstrakt: |
Attaining molecular- level control over solidification processes is a crucial aspect of materials science. To control ice formation, organisms have evolved bewildering arrays of ice- binding proteins (IBPs), but these have poorly understood structure--activity relationships. We propose that reverse engineering using de novo computational protein design can shed light on structure--activity relationships of IBPs. We hypothesized that the model alpha- helical winter flounder antifreeze protein uses an unusual undertwisting of its alpha- helix to align its putative ice- binding threonine residues in exactly the same direction. We test this hypothesis by designing a series of straight three- helix bundles with an ice- binding helix projecting threonines and two supporting helices constraining the twist of the ice- binding helix. Our findings show that ice- recrystallization inhibition by the designed proteins increases with the degree of designed undertwisting, thus validating our hypothesis, and opening up avenues for the computational design of IBPs. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
| Externí odkaz: |
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