Abstract
AbstractThe use of high‐resolution nmr to determine the structure of linear homo‐oligopeptides in solution is described. Complete assignments of NH and α‐CH resonances were elucidated based upon a guest–host series of compounds and selective α‐deuteration of residues in the chain. The conformations for oligomethionines and oligoglutamates in dimethylsulfoxide, chloroform, and trifluoroethanol are discussed, and molecular models are described. Recent studies of L‐glutamate peptides attached to polyoxyethylene are also included. These peptide–polyoxyethylene conjugates are soluble in a broad range of solvents, such as dimethyl‐sulfoxide, chloroform, trifluoroethanol, and water. Preliminary conclusions are drawn concerning the effects of amine terminal end groups and the nature of the solvent on the conformations of these peptide derivatives.
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