Ontology highlight
ABSTRACT:
SUBMITTER: Kritzer JA
PROVIDER: S-EPMC2857645 | biostudies-literature | 2005 Mar
REPOSITORIES: biostudies-literature
Journal of the American Chemical Society 20050301 12
We recently reported a beta-peptide foldamer, beta53-1, that folds into a 14-helix in aqueous solution, binds the oncoprotein hDM2 with submicromolar affinity, and potently inhibits the interaction of hDM2 with a peptide derived from the activation domain of p53 (p53AD). Here, we present the solution structure of beta53-1 in methanol. Details of the structure illustrate fundamental and novel elements of beta-peptide folding and recognition. These elements include the detailed arrangement of a co ...[more]