NMR Methods Used to Derive Solution Conformations in Peptides
This chapter discusses nuclear magnetic resonance (NMR) methods used to derive solution conformations in peptides. Two-dimensional proton NMR spectroscopy provides an important tool for identifying preferred conformers in otherwise unstructured peptides. This stems from its usefulness in detecting highly localized conformations that are not easily observable by other methods and from its ability to identify the particular residues involved in a given conformation. NMR can be used to discern conformations that resemble regular secondary structures of proteins, such as helices and tight turns, based primarily on NOE patterns and occasionally on coupling constants and amide-proton temperature-shift coefficients. Conformations that are less common in proteins such as backbone kinks or cis peptide bonds can also be inferred. In characterizing conformations, however, it must be appreciated that a peptide is frequently in dynamical equilibrium between a large numbers of conformers. At any one time, the peptide population in solution contains multiple conformers, only some of which are revealed by NMR. © 1994, ACADEMIC PRESS, INC.
