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One Peptide Reveals the Two Faces of α-Helix Unfolding-Folding Dynamics.

J Phys Chem B. 2018; 
Jesus Catarina S H,Cruz Pedro F,Arnaut Luis G,Brito Rui M M,Serpa Ca
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Peptide Synthesis . The analogue of the C-peptide, RN80, was custom-synthesized by GenScript Corporation, at a purity Get A Quote

摘要

The understanding of fast folding dynamics of single α-helices comes mostly from studies on rationally designed peptides displaying sequences with high helical propensity. The folding/unfolding dynamics and energetics of α-helix conformations in naturally occurring peptides remains largely unexplored. Here we report the study of a protein fragment analogue of the C-peptide from bovine pancreatic ribonuclease-A, RN80, a 13-amino acid residue peptide that adopts a highly populated helical conformation in aqueous solution. H NMR and CD structural studies of RN80 showed that α-helix formation displays a pH-dependent bell-shaped curve, with a maximum near pH 5, and a large decrease in helical content in a... More

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