Hydrogen bond surrogate stabilized water soluble 310-helix from a disordered pentapeptide containing coded α-amino acids
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Add time:08/23/2019 Source:sciencedirect.com
Replacing a hypothetical i + 3 → i peptide H-bond in a disordered pentapeptide, that lacks any helicogenic Cα-tetrasubstituted residues, with a propyl linker and carbamylating the N-terminal nitrogen constrains it in the elusive 310-helical structure with high helicity and stability under varying conditions of temperature and pH, confirmed by NMR and CD analyses.
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