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Bulky dehydroamino acids, beta-hairpins, cyana, NOESY, proteolysis
Bulky α,β-dehydroamino acids (ΔAAs) can improve the proteolytic stability of peptides that contain them, presumably by altering the shape of the backbone of the peptide and by stabilizing folded states through their rigidifying effect. The stabilizing effects of ΔAAs that contain at least one hydrogen atom at the β-carbon are well-known, but the role of bulky ΔAAs that contain fully substituted β-carbons in the stability of larger peptides is less explored. To better explore the conformational contribution of α,β-dehydroamino acids in β-hairpins we performed NMR-based structural calculations to confirm our experimental observations. We used the simulated annealing program CYANA to determine 20 low-energy conformations based on our NMR chemical shift and NOE data. The lowest energy conformations were then optimized using the quantum mechanics ONIOM method via the program Gaussian to confirm the hydrogen bonding pattern and the observed dihedral angles. The effect of the type and position of the bulky dehydroamino acid will be discussed.
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BYU ScholarsArchive Citation
Kastner, David W.; Jalan, Ankur; and Castle, Steven L., "Computational Predictions of β-Hairpins Containing Bulky Dehydroamino Acids" (2017). Library Undergraduate Poster Competition 2017. 4.
Physiology and Developmental Biology
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