Structural Properties of Substituted Mucin Peptides in Solution by 2D NMR

Abstract

The short mucin peptide with the sequence Glycine-Valine-Threonine-Serine-Alanine-Proline-Aspartic acid has been shown to have significant interactions with a specific monoclonal antibody. Its proline residue appears to be required for the binding. To explore the function of proline further, the structures of three substituted mucin peptides were studied. Two-dimensional nuclear magnetic resonance (2D NMR) was employed to study the structures of these peptides in aqueous solution.