Effect of charged amino acid side chain length at non-hydrogen bonded strand positions on β-hairpin stability.

摘要: β-Sheets have been implicated in various neurological disorders, and ∼20% of protein residues adopt a sheet conformation. Therefore, studies on the structural origin stability can provide fundamental knowledge with potential biomedical applications. Oppositely charged amino acids are frequently observed across one another antiparallel β-sheets. Interestingly, side chains natural Asp, Glu, Arg, Lys different numbers hydrophobic methylenes linking backbone to hydrophilic functionalities. To explore inherent effect acid chain length sheets, designed hairpin motif containing varying lengths at non-hydrogen bonded positions was studied. Peptides guest position N-terminal strand C-terminal were investigated by NMR methods. The (Xaa) included negatively carboxylate group (Asp, Glu,...